Structure of ubiquitin-fold modifier 1-specific protease UfSP2

Title
Structure of ubiquitin-fold modifier 1-specific protease UfSP2
Authors
하병학전영주신상철Kanako TatsumiMasaaki KomatsuKeiji TanakaChristopher M. WatsoGillian WallisChin Ha Chung김은경
Issue Date
2011-03
Publisher
The Journal of biological chemistry
Citation
VOL 286, NO 12, 10248-10257
Abstract
Ubiquitin-fold modifier 1 (Ufm1)-specific protease 2 (UfSP2) is a cysteine protease that is responsible for the release of Ufm1 from Ufm1-conjugated cellular proteins, as well as for the generation of mature Ufm1 from its precursor. The 2.6Å resolution crystal structure of mouse UfSP2 reveals that it is composed of two domains. The C-terminal catalytic domain is similar to UfSP1 with Cys294, Asp418, His420, Tyr282, and a regulatory loop participating in catalysis. The novel N-terminal domain shows a unique structure and plays a role in the recognition of its cellular substrate C20orf116 and thus in the recruitment of UfSP2 to the endoplasmic reticulum, where C20orf116 predominantly localizes. Mutagenesis studies were carried out to provide the structural basis for understanding the loss of catalytic activity observed in a recently identified UfSP2 mutation that is associated with an autosomal dominant form of hip dysplasia.
URI
http://pubs.kist.re.kr/handle/201004/41051
ISSN
0021-9258
Appears in Collections:
KIST Publication > Article
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE