{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/21483"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/21483","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"1. X-ray crystallographic analyses of the gene V protein from Ff bacteriophage, a single-stranded DNA-binding protein, and its Y41 mutants 2. X-ray crystallographic analyses of several anticancer drugs and their interactions with DNA","abstract":"In biological systems, DNA/RNA-protein interactions as well as drug-DNA interactions play important roles in genetic processes. A fundamental understanding of these processes requires a detailed structural knowledge of DNAs, proteins, drugs, as well as their complexes with each other. Gene V protein (GVP) encoded by the filamentous bacteriophage Ff (M13, f1, fd) is a single-stranded DNA (ssDNA) binding protein which binds to ssDNA non-specifically and cooperatively. The structure of the wild-type protein has been determined and refined at 1.8A resolution (Skinner et al., (1994) Proc. Natl. Acad. Sci. USA. 91, 2071-2075). It is largely composed of $\\beta$-structure with three prominent loops: DNA-binding loop, dyad loop and dimer contact loop. Y41 plays an essential role in the dimer-dimer interactions of the protein-ssDNA complex. Two Y41 mutant structures, namely Y41F and Y41H, have been studied by X-ray crystallography to high resolution. Y41F GVP crystallized isomorphously to the wild-type, while Y41H GVP crystallized in a different space group (P2$\\sb12\\sb12\\sb1).$ Y41H GVP structure has been solved by the molecular replacement method. In both crystals, the loop (residues 36-43) that contains residue 41 is involved in the crystal dimer packings, but in a different manner. Using the crystal packing infomations as guidance, we were able to construct the GVP-ssDNA complex model, consistent with existing biochemical and biophysical data.","abstract_html":"In biological systems, DNA/RNA-protein interactions as well as drug-DNA interactions play important roles in genetic processes. A fundamental understanding of these processes requires a detailed structural knowledge of DNAs, proteins, drugs, as well as their complexes with each other. Gene V protein (GVP) encoded by the filamentous bacteriophage Ff (M13, f1, fd) is a single-stranded DNA (ssDNA) binding protein which binds to ssDNA non-specifically and cooperatively. The structure of the wild-type protein has been determined and refined at 1.8A resolution (Skinner et al., (1994) Proc. Natl. Acad. Sci. USA. 91, 2071-2075). It is largely composed of <span class=\"etd-inline-math\">&beta;</span>-structure with three prominent loops: DNA-binding loop, dyad loop and dimer contact loop. Y41 plays an essential role in the dimer-dimer interactions of the protein-ssDNA complex. Two Y41 mutant structures, namely Y41F and Y41H, have been studied by X-ray crystallography to high resolution. Y41F GVP crystallized isomorphously to the wild-type, while Y41H GVP crystallized in a different space group (P2$\\sb12\\sb12\\sb1).$ Y41H GVP structure has been solved by the molecular replacement method. In both crystals, the loop (residues 36-43) that contains residue 41 is involved in the crystal dimer packings, but in a different manner. Using the crystal packing infomations as guidance, we were able to construct the GVP-ssDNA complex model, consistent with existing biochemical and biophysical data.","abstract_has_math":true,"creators":["Guan, Yue"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biophysics","degree_department":null,"school":null,"contributors":["Wang, Andrew H.J.","Wraight, Colin A.","Churchill, Mair"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T13:09:54Z","date_published":"2011-05-07T13:09:54Z","updated_at":"2026-07-22T22:25:18Z","subjects":["Biology, Molecular","Chemistry, Pharmaceutical","Health Sciences, Pharmacy","Biophysics, Medical","Health Sciences, Oncology"],"languages":["eng"],"rights":["Copyright 1994 Yue Guan"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9512380","(UMI)AAI9512380"],"render_values":[{"text":"AAI9512380","href":null,"code":true},{"text":"(UMI)AAI9512380","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/21483","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Wang, Andrew H.J.","Wraight, Colin A.","Churchill, Mair"]},{"key":"dc:creator","label":"Author","values":["Guan, Yue"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T13:09:54Z","10000-01-01","1994"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biophysics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, Molecular","Chemistry, Pharmaceutical","Health Sciences, Pharmacy","Biophysics, Medical","Health Sciences, Oncology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1994 Yue Guan"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["AAI9512380","(UMI)AAI9512380","http://hdl.handle.net/2142/21483"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["In biological systems, DNA/RNA-protein interactions as well as drug-DNA interactions play important roles in genetic processes. A fundamental understanding of these processes requires a detailed structural knowledge of DNAs, proteins, drugs, as well as their complexes with each other. Gene V protein (GVP) encoded by the filamentous bacteriophage Ff (M13, f1, fd) is a single-stranded DNA (ssDNA) binding protein which binds to ssDNA non-specifically and cooperatively. The structure of the wild-type protein has been determined and refined at 1.8A resolution (Skinner et al., (1994) Proc. Natl. Acad. Sci. USA. 91, 2071-2075). It is largely composed of $\\beta$-structure with three prominent loops: DNA-binding loop, dyad loop and dimer contact loop. Y41 plays an essential role in the dimer-dimer interactions of the protein-ssDNA complex. Two Y41 mutant structures, namely Y41F and Y41H, have been studied by X-ray crystallography to high resolution. Y41F GVP crystallized isomorphously to the wild-type, while Y41H GVP crystallized in a different space group (P2$\\sb12\\sb12\\sb1).$ Y41H GVP structure has been solved by the molecular replacement method. In both crystals, the loop (residues 36-43) that contains residue 41 is involved in the crystal dimer packings, but in a different manner. Using the crystal packing infomations as guidance, we were able to construct the GVP-ssDNA complex model, consistent with existing biochemical and biophysical data.","Several drug molecules such as ecteinascidins and UK63052, are potent anticancer drugs. The high resolution crystal structural analyses as well as the modeling studies of these molecules provide us with valuable information on how these molecules exert their functions in the living cells. Cyclic ribodiguanylic acid, c-(GpGp), is the endogenous effector regulator of cellulose synthase. Their structural analyses help us in understanding the structure-function relationship of cyclic-DNA/RNAs.","Made available in DSpace on 2011-05-07T13:09:54Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9512380.pdf: 6179417 bytes, checksum: f89db32fb337fcaee5e58531eb72b63d (MD5) Previous issue date: 1994","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:51:05Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:23:25-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"]},{"key":"dc:title","label":"Title","values":["1. X-ray crystallographic analyses of the gene V protein from Ff bacteriophage, a single-stranded DNA-binding protein, and its Y41 mutants 2. X-ray crystallographic analyses of several anticancer drugs and their interactions with DNA"]}]}],"canonical_facts":{"dc:contributor":["Wang, Andrew H.J.","Wraight, Colin A.","Churchill, Mair"],"dc:creator":["Guan, Yue"],"dc:date":["2011-05-07T13:09:54Z","10000-01-01","1994"],"dc:description":["In biological systems, DNA/RNA-protein interactions as well as drug-DNA interactions play important roles in genetic processes. A fundamental understanding of these processes requires a detailed structural knowledge of DNAs, proteins, drugs, as well as their complexes with each other. Gene V protein (GVP) encoded by the filamentous bacteriophage Ff (M13, f1, fd) is a single-stranded DNA (ssDNA) binding protein which binds to ssDNA non-specifically and cooperatively. The structure of the wild-type protein has been determined and refined at 1.8A resolution (Skinner et al., (1994) Proc. Natl. Acad. Sci. USA. 91, 2071-2075). It is largely composed of $\\beta$-structure with three prominent loops: DNA-binding loop, dyad loop and dimer contact loop. Y41 plays an essential role in the dimer-dimer interactions of the protein-ssDNA complex. Two Y41 mutant structures, namely Y41F and Y41H, have been studied by X-ray crystallography to high resolution. Y41F GVP crystallized isomorphously to the wild-type, while Y41H GVP crystallized in a different space group (P2$\\sb12\\sb12\\sb1).$ Y41H GVP structure has been solved by the molecular replacement method. In both crystals, the loop (residues 36-43) that contains residue 41 is involved in the crystal dimer packings, but in a different manner. Using the crystal packing infomations as guidance, we were able to construct the GVP-ssDNA complex model, consistent with existing biochemical and biophysical data.","Several drug molecules such as ecteinascidins and UK63052, are potent anticancer drugs. The high resolution crystal structural analyses as well as the modeling studies of these molecules provide us with valuable information on how these molecules exert their functions in the living cells. Cyclic ribodiguanylic acid, c-(GpGp), is the endogenous effector regulator of cellulose synthase. Their structural analyses help us in understanding the structure-function relationship of cyclic-DNA/RNAs.","Made available in DSpace on 2011-05-07T13:09:54Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9512380.pdf: 6179417 bytes, checksum: f89db32fb337fcaee5e58531eb72b63d (MD5) Previous issue date: 1994","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:51:05Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:23:25-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"],"dc:identifier":["AAI9512380","(UMI)AAI9512380","http://hdl.handle.net/2142/21483"],"dc:language":["eng"],"dc:rights":["Copyright 1994 Yue Guan"],"dc:subject":["Biology, Molecular","Chemistry, Pharmaceutical","Health Sciences, Pharmacy","Biophysics, Medical","Health Sciences, Oncology"],"dc:title":["1. X-ray crystallographic analyses of the gene V protein from Ff bacteriophage, a single-stranded DNA-binding protein, and its Y41 mutants 2. X-ray crystallographic analyses of several anticancer drugs and their interactions with DNA"],"dc:type":["text"],"thesis:degree_discipline":["Biophysics"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:18Z"}