1w6v

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SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15

Overview

Ubiquitin-specific proteases (USPs) can remove covalently attached, ubiquitin moieties from target proteins and regulate both the stability, and ubiquitin-signaling state of their substrates. All USPs contain a, conserved catalytic domain surrounded by one or more subdomains, some of, which contribute to target recognition. One such specific subdomain, the, DUSP domain (domain present in ubiquitin-specific proteases), is present, in at least seven different human USPs that regulate the stability of or, interact with the hypoxia-inducible transcription factor HIF1-alpha, the, Von Hippel-Lindau protein (pVHL), cullin E3 ligases, and BRCA2. We, describe the NMR solution structure of the DUSP domain of human USP15, recently implicated in COP9 (constitutive photomorphogenic gene, 9)-signalosome regulation. Its tripod-like structure consists of a 3-fold, alpha-helical bundle supporting a triple-stranded anti-parallel, beta-sheet. The DUSP domain displays a novel fold, an alpha/beta tripod, (AB3). DUSP domain surface properties and previously described work, suggest a potential role in protein/protein interaction or substrate, recognition.

About this Structure

1W6V is a Single protein structure of sequence from Homo sapiens. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 Full crystallographic information is available from OCA.

Reference

Solution structure of the human ubiquitin-specific protease 15 DUSP domain., de Jong RN, Ab E, Diercks T, Truffault V, Daniels M, Kaptein R, Folkers GE, J Biol Chem. 2006 Feb 24;281(8):5026-31. Epub 2005 Nov 18. PMID:16298993

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