Ontology highlight
ABSTRACT:
SUBMITTER: Wang W
PROVIDER: S-EPMC3135737 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Wang Wei W Liu Lijun L Song Xi X Mo Yi Y Komma Chandrasekhar C Bellamy Henry D HD Zhao Zhizhuang Joe ZJ Zhou G Wayne GW
Journal of cellular biochemistry 20110801 8
SHP-1 belongs to the family of non-receptor protein tyrosine phosphatases (PTPs) and generally acts as a negative regulator in a variety of cellular signaling pathways. Previously, the crystal structures of the tail-truncated SHP-1 and SHP-2 revealed an autoinhibitory conformation. To understand the regulatory mechanism of SHP-1, we have determined the crystal structure of the full-length SHP-1 at 3.1 Å. Although the tail was disordered in current structure, the huge conformational rearrangement ...[more]