Structure of ubiquitin-fold modifier 1-specific protease UfSP2
- Structure of ubiquitin-fold modifier 1-specific protease UfSP2
- 하병학; 전영주; 신상철; Kanako Tatsumi; Masaaki Komatsu; Keiji Tanaka; Christopher M. Watso; Gillian Wallis; Chin Ha Chung; 김은경
- Issue Date
- The Journal of biological chemistry
- VOL 286, NO 12, 10248-10257
- 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.
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