1nb8: Difference between revisions

Revision as of 14:21, 27 July 2008

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File:1nb8.png

Template:STRUCTURE 1nb8

Structure of the catalytic domain of USP7 (HAUSP)Structure of the catalytic domain of USP7 (HAUSP)

Template:ABSTRACT PUBMED 12507430

About this StructureAbout this Structure

1NB8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde., Hu M, Li P, Li M, Li W, Yao T, Wu JW, Gu W, Cohen RE, Shi Y, Cell. 2002 Dec 27;111(7):1041-54. PMID:12507430

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Structure of the catalytic domain of USP7 (HAUSP)'''
+===Structure of the catalytic domain of USP7 (HAUSP)===
-==Overview==
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-The ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an essential role in numerous cellular processes. HAUSP, a representative UBP, specifically deubiquitinates and hence stabilizes the tumor suppressor protein p53. Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde. These studies reveal that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm, and Thumb. The leaving ubiquitin moiety is specifically coordinated by the Fingers, with its C terminus placed in the active site between the Palm and the Thumb. Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad residues for catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12507430}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12507430}}
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 [[Category: P53 binding]]
 [[Category: Ubp]]
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