2gfo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gfo.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2gfo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gfo| PDB=2gfo | SCENE= }}
{{STRUCTURE_2gfo| PDB=2gfo | SCENE= }}
-
'''Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8'''
+
===Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8===
-
==Overview==
+
<!--
-
Ubiquitin-specific protease 8 (USP8) hydrolyzes mono and polyubiquitylated targets such as epidermal growth factor receptors and is involved in clathrin-mediated internalization. In 1182 residues, USP8 contains multiple domains, including coiled-coil, rhodanese, and catalytic domains. We report the first high-resolution crystal structures of these domains and discuss their implications for USP8 function. The amino-terminal domain is a homodimer with a novel fold. It is composed of two five-helix bundles, where the first helices are swapped, and carboxyl-terminal helices are extended in an antiparallel fashion. The structure of the rhodanese domain, determined in complex with the E3 ligase NRDP1, reveals the canonical rhodanese fold but with a distorted primordial active site. The USP8 recognition domain of NRDP1 has a novel protein fold that interacts with a conserved peptide loop of the rhodanese domain. A consensus sequence of this loop is found in other NRDP1 targets, suggesting a common mode of interaction. The structure of the carboxyl-terminal catalytic domain of USP8 exhibits the conserved tripartite architecture but shows unique traits. Notably, the active site, including the ubiquitin binding pocket, is in a closed conformation, incompatible with substrate binding. The presence of a zinc ribbon subdomain near the ubiquitin binding site further suggests a polyubiquitin-specific binding site and a mechanism for substrate induced conformational changes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17035239}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17035239 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17035239}}
==About this Structure==
==About this Structure==
Line 45: Line 49:
[[Category: Ubl conjugation pathway]]
[[Category: Ubl conjugation pathway]]
[[Category: Zinc ribbon]]
[[Category: Zinc ribbon]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:03:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:16:19 2008''

Revision as of 08:16, 28 July 2008

Image:2gfo.png

Template:STRUCTURE 2gfo

Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8

Template:ABSTRACT PUBMED 17035239

About this Structure

2GFO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)., Avvakumov GV, Walker JR, Xue S, Finerty PJ Jr, Mackenzie F, Newman EM, Dhe-Paganon S, J Biol Chem. 2006 Dec 8;281(49):38061-70. Epub 2006 Oct 11. PMID:17035239

Page seeded by OCA on Mon Jul 28 11:16:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gfo"
Personal tools