NPM1 IS A MULTIFUNCTIONAL PHOSPHOPROTEIN WHICH SHUTTLES BETWEEN NUCLEUS AND CYTOPLASM. WHEN NPM1 INTERACTS WITH P53, A MUTATION IN ITS C-TERMINUS LEADS TO SEQUESTRATION OF P53 INTO CYTOPLASM, PREVENTING IT FROM GOING INTO THE NUCLEUS. WE HAVE CARRIED OUT STRUCTURAL STUDIES ON THE 53 RESIDUE C-TERMINAL DOMAIN OF HUMAN NPM1, WHICH COMPRISES AN AROMATIC RICH REGION, CONTAINING TWO TRYPTOPHAN RESIDUES. USING NMR, WE FOUND THAT THE C-TERMINAL DOMAIN OF NPM1 IS MADE UP OF 3 ALPHA-HELICES, EACH ENCOMPASSING 10-12 AMINO ACIDS. IT FORMS A TERTIARY STRUCTURE RESEMBLING A TRIANGLE WITH N AND C-TERMINI OF THE DOMAIN COMING TOGETHER. THIS STRUCTURE WILL SERVE AS A PEDESTAL TOWARDS MAPPING THE REGIONS IN NPM1 INVOLVED IN BINDING TO P53. THE INFORMATION OBTAINED WILL PROVIDE AN INSIGHT INTO DEVELOPMENT OF SMALL-MOLECULE DRUGS WHICH COULD PREVENT THE BINDING OF NPM TO P53 AND ALLOWING IT TO CARRY OUT ITS TRANSCRIPTIONAL FUNCTION LEADING TO APOPTOSIS.
","abstract_html":"<P>NPM1 IS A MULTIFUNCTIONAL PHOSPHOPROTEIN WHICH SHUTTLES BETWEEN NUCLEUS AND CYTOPLASM. WHEN NPM1 INTERACTS WITH P53, A MUTATION IN ITS C-TERMINUS LEADS TO SEQUESTRATION OF P53 INTO CYTOPLASM, PREVENTING IT FROM GOING INTO THE NUCLEUS. WE HAVE CARRIED OUT STRUCTURAL STUDIES ON THE 53 RESIDUE C-TERMINAL DOMAIN OF HUMAN NPM1, WHICH COMPRISES AN AROMATIC RICH REGION, CONTAINING TWO TRYPTOPHAN RESIDUES. USING NMR, WE FOUND THAT THE C-TERMINAL DOMAIN OF NPM1 IS MADE UP OF 3 ALPHA-HELICES, EACH ENCOMPASSING 10-12 AMINO ACIDS. IT FORMS A TERTIARY STRUCTURE RESEMBLING A TRIANGLE WITH N AND C-TERMINI OF THE DOMAIN COMING TOGETHER. THIS STRUCTURE WILL SERVE AS A PEDESTAL TOWARDS MAPPING THE REGIONS IN NPM1 INVOLVED IN BINDING TO P53. THE INFORMATION OBTAINED WILL PROVIDE AN INSIGHT INTO DEVELOPMENT OF SMALL-MOLECULE DRUGS WHICH COULD PREVENT THE BINDING OF NPM TO P53 AND ALLOWING IT TO CARRY OUT ITS TRANSCRIPTIONAL FUNCTION LEADING TO APOPTOSIS. </P>","abstract_has_math":false,"creators":["AMBALIKA SAGARIKA KHADRIA"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2008,"date_issued":"2008-11-03","date_published":"2008-11-03","updated_at":"2026-07-24T03:31:51Z","subjects":["NPM1, AML, p53, NMR, apoptosis, CNS"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["AMBALIKA SAGARIKA KHADRIA"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["2008-11-03"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://scholarbank.nus.edu.sg/handle/10635/161025"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["NPM1, AML, p53, NMR, apoptosis, CNS"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://scholarbank.nus.edu.sg/bitstreams/a286e3f6-eb32-4bf4-82b6-71c3f074f08e/download"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["NPM1 IS A MULTIFUNCTIONAL PHOSPHOPROTEIN WHICH SHUTTLES BETWEEN NUCLEUS AND CYTOPLASM. WHEN NPM1 INTERACTS WITH P53, A MUTATION IN ITS C-TERMINUS LEADS TO SEQUESTRATION OF P53 INTO CYTOPLASM, PREVENTING IT FROM GOING INTO THE NUCLEUS. WE HAVE CARRIED OUT STRUCTURAL STUDIES ON THE 53 RESIDUE C-TERMINAL DOMAIN OF HUMAN NPM1, WHICH COMPRISES AN AROMATIC RICH REGION, CONTAINING TWO TRYPTOPHAN RESIDUES. USING NMR, WE FOUND THAT THE C-TERMINAL DOMAIN OF NPM1 IS MADE UP OF 3 ALPHA-HELICES, EACH ENCOMPASSING 10-12 AMINO ACIDS. IT FORMS A TERTIARY STRUCTURE RESEMBLING A TRIANGLE WITH N AND C-TERMINI OF THE DOMAIN COMING TOGETHER. THIS STRUCTURE WILL SERVE AS A PEDESTAL TOWARDS MAPPING THE REGIONS IN NPM1 INVOLVED IN BINDING TO P53. THE INFORMATION OBTAINED WILL PROVIDE AN INSIGHT INTO DEVELOPMENT OF SMALL-MOLECULE DRUGS WHICH COULD PREVENT THE BINDING OF NPM TO P53 AND ALLOWING IT TO CARRY OUT ITS TRANSCRIPTIONAL FUNCTION LEADING TO APOPTOSIS.
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"],"dc:format.checksum.md5":["e333d586923cf79b836133e99e0d79e1","ff191afb74566e11d0e24936244a379b"],"dc:identifier.uri":["https://scholarbank.nus.edu.sg/bitstreams/a286e3f6-eb32-4bf4-82b6-71c3f074f08e/download"],"dc:relation.isreferencedby":["https://scholarbank.nus.edu.sg/handle/10635/161025"],"dc:subject":["NPM1, AML, p53, NMR, apoptosis, CNS"],"dc:title":["Structural characterization of the C-terminal domain of human nucleophosmin, NPM1"],"dc:type":["Thesis"]},"updated_at":"2026-07-24T03:31:51Z"}