1zo6: Difference between revisions

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~~{{Theoretical_model}}~~

==NMR BASED MODEL OF LYS48-LINKED DI-UBIQUITIN COMPLEX WITH C- TERMINAL UBA DOMAIN OF HHR23A==

== Structural highlights ==

<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZO6 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zo6 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1zo6 PDBsum]</span></td></tr>

<table>

== 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.

~~[[Image~~:~~1zo6~~.~~png|left|200px]]~~

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>

~~{{STRUCTURE_1zo6| PDB=1zo6 | SCENE= }}~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~===NMR BASED MODEL OF LYS48-LINKED DI-UBIQUITIN COMPLEX WITH C- TERMINAL UBA DOMAIN OF HHR23A===~~

== References ==

~~{{ABSTRACT_PUBMED_15949443}}~~

__TOC__

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:015949443<~~/~~ref><ref group="xtra">PMID:019773779</ref~~><~~references group="xtra"~~/>

[[Category: Assfalg, M]]

[[Category: Fushman, D]]

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@@ Line 1: / Line 1: @@
-{{Theoretical_model}}
+==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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZO6 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zo6 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1zo6 PDBsum]</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.
-[[Image:1zo6.png|left|200px]]
+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>
-{{STRUCTURE_1zo6|  PDB=1zo6  |  SCENE=  }}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-===NMR BASED MODEL OF LYS48-LINKED DI-UBIQUITIN COMPLEX WITH C- TERMINAL UBA DOMAIN OF HHR23A===
+== References ==
+<references/>
-{{ABSTRACT_PUBMED_15949443}}
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:015949443</ref><ref group="xtra">PMID:019773779</ref><references group="xtra"/>
 [[Category: Assfalg, M]]
 [[Category: Fushman, D]]