3PS5

Crystal structure of the full-length Human Protein Tyrosine Phosphatase SHP-1

3PS5 の概要

• エントリーDOI: 10.2210/pdb3ps5/pdb
• 分子名称: Tyrosine-protein phosphatase non-receptor type 6, SULFATE ION (3 entities in total)
• 機能のキーワード: sh2, ptp, phosphatase, hydrolase, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P29350
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68120.30

構造登録者

Wang, W.,Liu, L.,Song, X.,Mo, Y.,Komma, C.,Bellamy, H.D.,Zhao, Z.J.,Zhou, G.W. (登録日: 2010-11-30, 公開日: 2011-04-20, 最終更新日: 2023-09-06)

主引用文献

Wang, W.,Liu, L.,Song, X.,Mo, Y.,Komma, C.,Bellamy, H.D.,Zhao, Z.J.,Zhou, G.W.
Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation.
J.Cell.Biochem., 112:2062-2071, 2011

PubMed Abstract: 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.

PubMed: 21465528
DOI: 10.1002/jcb.23125

実験手法

X-RAY DIFFRACTION (3.1 Å)