{"id":{"repo_id":"aachen","oai_identifier":"oai:publications.rwth-aachen.de:59866"},"canonical_url":"https://search.dev.ndltd.org/etd/aachen/oai:publications.rwth-aachen.de:59866","repository":{"repo_id":"aachen","name":"RWTH Aachen University","base_url":"https://publications.rwth-aachen.de/oai2d"},"display":{"title":"Bestimmung der Lösungsstruktur der dritten Extrazellulärdomäne des Signaltransduktors gp130 mittels mehrdimensionaler heteronuklearer NMR-Spektroskopie","abstract":"The signal transducer gp130: Solution structure of the carboxy-terminal domain of the cytokin receptor homology region. The transmembrane glycoprotein gp130 is the common signal transducing receptor subunit of the interleukin-6-type cytokines. It is a member of the cytokin-receptor superfamily predicted to consist of six domains in its extracellular part. The second and the third domain constitute the cytokine-binding module defined by a set of four conserved cysteines and a WSXWS motif, respectively. The three-dimensional structure of the carboxy-terminal domain of this region was determined by multidimensional NMR. The domain consists of seven beta-strands constituting a fibronectin type-III like topology. The structure reveals that the WSDWS motif of gp130 is part of an extended tryptophan/arginine zipper which modulates the conformation of the CD-loop.","abstract_html":"The signal transducer gp130: Solution structure of the carboxy-terminal domain of the cytokin receptor homology region. The transmembrane glycoprotein gp130 is the common signal transducing receptor subunit of the interleukin-6-type cytokines. It is a member of the cytokin-receptor superfamily predicted to consist of six domains in its extracellular part. The second and the third domain constitute the cytokine-binding module defined by a set of four conserved cysteines and a WSXWS motif, respectively. The three-dimensional structure of the carboxy-terminal domain of this region was determined by multidimensional NMR. The domain consists of seven beta-strands constituting a fibronectin type-III like topology. The structure reveals that the WSDWS motif of gp130 is part of an extended tryptophan/arginine zipper which modulates the conformation of the CD-loop.","abstract_has_math":false,"creators":["Kernebeck, Thomas"],"institution":"Publikationsserver der RWTH Aachen University","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Grötzinger, Joachim"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2000,"date_issued":"2000","date_published":"2000","updated_at":"2026-07-30T19:42:48Z","subjects":["info:eu-repo/classification/ddc/540","Chemie","Cytokine","Rezeptor","Signaltransduktion","Extrazellulärraum","Domäne","Mehrdimensionale NMR-Spektroskopie"],"languages":["ger"],"rights":["info:eu-repo/semantics/openAccess"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-121611%22"],"render_values":[{"text":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-121611%22","href":"https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-121611%22","code":true}]}]},"links":{"outbound_url":"https://publications.rwth-aachen.de/record/59866","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Grötzinger, Joachim"]},{"key":"dc:creator","label":"Author","values":["Kernebeck, Thomas"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:coverage","label":"Dc Coverage","values":["DE"]},{"key":"dc:date","label":"Dc Date","values":["2000"]},{"key":"dc:publisher","label":"Institution","values":["Publikationsserver der RWTH Aachen University"]},{"key":"dc:relation","label":"Dc Relation","values":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-1404"]},{"key":"dc:type","label":"Dc Type","values":["info:eu-repo/semantics/doctoralThesis","info:eu-repo/semantics/publishedVersion"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["info:eu-repo/classification/ddc/540","Chemie","Cytokine","Rezeptor","Signaltransduktion","Extrazellulärraum","Domäne","Mehrdimensionale NMR-Spektroskopie"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["ger"]},{"key":"dc:rights","label":"Dc Rights","values":["info:eu-repo/semantics/openAccess"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://publications.rwth-aachen.de/record/59866","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-121611%22"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The signal transducer gp130: Solution structure of the carboxy-terminal domain of the cytokin receptor homology region. The transmembrane glycoprotein gp130 is the common signal transducing receptor subunit of the interleukin-6-type cytokines. It is a member of the cytokin-receptor superfamily predicted to consist of six domains in its extracellular part. The second and the third domain constitute the cytokine-binding module defined by a set of four conserved cysteines and a WSXWS motif, respectively. The three-dimensional structure of the carboxy-terminal domain of this region was determined by multidimensional NMR. The domain consists of seven beta-strands constituting a fibronectin type-III like topology. The structure reveals that the WSDWS motif of gp130 is part of an extended tryptophan/arginine zipper which modulates the conformation of the CD-loop."]},{"key":"dc:source","label":"Dc Source","values":["Aachen : Publikationsserver der RWTH Aachen University II, 98 S. : Ill., graph. Darst. (2000). = Aachen, Techn. Hochsch., Diss., 2000"]},{"key":"dc:title","label":"Title","values":["Bestimmung der Lösungsstruktur der dritten Extrazellulärdomäne des Signaltransduktors gp130 mittels mehrdimensionaler heteronuklearer NMR-Spektroskopie"]}]}],"canonical_facts":{"dc:contributor":["Grötzinger, Joachim"],"dc:coverage":["DE"],"dc:creator":["Kernebeck, Thomas"],"dc:date":["2000"],"dc:description":["The signal transducer gp130: Solution structure of the carboxy-terminal domain of the cytokin receptor homology region. The transmembrane glycoprotein gp130 is the common signal transducing receptor subunit of the interleukin-6-type cytokines. It is a member of the cytokin-receptor superfamily predicted to consist of six domains in its extracellular part. The second and the third domain constitute the cytokine-binding module defined by a set of four conserved cysteines and a WSXWS motif, respectively. The three-dimensional structure of the carboxy-terminal domain of this region was determined by multidimensional NMR. The domain consists of seven beta-strands constituting a fibronectin type-III like topology. The structure reveals that the WSDWS motif of gp130 is part of an extended tryptophan/arginine zipper which modulates the conformation of the CD-loop."],"dc:identifier":["https://publications.rwth-aachen.de/record/59866","https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-121611%22"],"dc:language":["ger"],"dc:publisher":["Publikationsserver der RWTH Aachen University"],"dc:relation":["info:eu-repo/semantics/altIdentifier/urn/urn:nbn:de:hbz:82-opus-1404"],"dc:rights":["info:eu-repo/semantics/openAccess"],"dc:source":["Aachen : Publikationsserver der RWTH Aachen University II, 98 S. : Ill., graph. Darst. (2000). = Aachen, Techn. 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