1zo6: Difference between revisions
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==NMR BASED MODEL OF LYS48-LINKED DI-UBIQUITIN COMPLEX WITH C- TERMINAL UBA DOMAIN OF HHR23A== | |||
<StructureSection load='1zo6' size='340' side='right'caption='[[1zo6]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZO6 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zo6 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1zo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zo6 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Although functional diversity in polyubiquitin chain signaling has been ascribed to the ability of differently linked chains to bind in a distinctive manner to effector proteins, structural models of such interactions have been lacking. Here, we use NMR to unveil the structural basis of selective recognition of Lys48-linked di- and tetraubiquitin chains by the UBA2 domain of hHR23A. Although the interaction of UBA2 with Lys48-linked diubiquitin involves the same hydrophobic surface on each ubiquitin unit as that utilized in monoubiquitin:UBA complexes, our results show how the "closed" conformation of Lys48-linked diubiquitin is crucial for high-affinity binding. Moreover, recognition of Lys48-linked diubiquitin involves a unique epitope on UBA, which allows the formation of a sandwich-like diubiqutin:UBA complex. Studies of the UBA-tetraubiquitin interaction suggest that this mode of UBA binding to diubiquitin is relevant for longer chains. | |||
Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain.,Varadan R, Assfalg M, Raasi S, Pickart C, Fushman D Mol Cell. 2005 Jun 10;18(6):687-98. PMID:15949443<ref>PMID:15949443</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zo6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
== | |||
< | |||
[[Category: Assfalg, M]] | [[Category: Assfalg, M]] | ||
[[Category: Fushman, D]] | [[Category: Fushman, D]] | ||
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[[Category: Raasi, S]] | [[Category: Raasi, S]] | ||
[[Category: Varadan, R]] | [[Category: Varadan, R]] | ||
Latest revision as of 11:22, 10 November 2021
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NMR BASED MODEL OF LYS48-LINKED DI-UBIQUITIN COMPLEX WITH C- TERMINAL UBA DOMAIN OF HHR23ANMR BASED MODEL OF LYS48-LINKED DI-UBIQUITIN COMPLEX WITH C- TERMINAL UBA DOMAIN OF HHR23A
Structural highlights
Publication Abstract from PubMedAlthough functional diversity in polyubiquitin chain signaling has been ascribed to the ability of differently linked chains to bind in a distinctive manner to effector proteins, structural models of such interactions have been lacking. Here, we use NMR to unveil the structural basis of selective recognition of Lys48-linked di- and tetraubiquitin chains by the UBA2 domain of hHR23A. Although the interaction of UBA2 with Lys48-linked diubiquitin involves the same hydrophobic surface on each ubiquitin unit as that utilized in monoubiquitin:UBA complexes, our results show how the "closed" conformation of Lys48-linked diubiquitin is crucial for high-affinity binding. Moreover, recognition of Lys48-linked diubiquitin involves a unique epitope on UBA, which allows the formation of a sandwich-like diubiqutin:UBA complex. Studies of the UBA-tetraubiquitin interaction suggest that this mode of UBA binding to diubiquitin is relevant for longer chains. Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain.,Varadan R, Assfalg M, Raasi S, Pickart C, Fushman D Mol Cell. 2005 Jun 10;18(6):687-98. PMID:15949443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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