| http://purl.uniprot.org/citations/21465528 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21465528 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21465528 | http://www.w3.org/2000/01/rdf-schema#comment | "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 of the N-SH2 domain and the incorporation of sulfate ions into the ligand-binding site of each domain indicate that the SHP-1 is in the open conformation. The N-SH2 domain in current structure is shifted away from the active site of the PTP domain to the other side of the C-SH2 domain, resulting in exposure of the active site. Meanwhile, the C-SH2 domain is twisted anticlockwise by about 110°. In addition, a set of new interactions between two SH2 domains and between the N-SH2 and the catalytic domains is identified, which could be responsible for the stabilization of SHP-1 in the open conformation. Based on the structural comparison, a model for the activation of SHP-1 is proposed."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcb.23125"xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcb.23125"xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Liu L."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Liu L."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Bellamy H.D."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Bellamy H.D."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Song X."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Song X."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Wang W."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Wang W."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Mo Y."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Mo Y."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Zhou G.W."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Zhou G.W."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Zhao Z.J."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Zhao Z.J."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Komma C."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/author | "Komma C."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/name | "J. Cell. Biochem."xsd:string |
| http://purl.uniprot.org/citations/21465528 | http://purl.uniprot.org/core/name | "J. Cell. Biochem."xsd:string |