4hjp | pdb_00004hjp

SHP-1 catalytic domain WPD loop open

spinqualitylabelsall models 4hjp, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hjp is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4hjq Gene: HCP, PTP1C, PTPN6, SHP-1 (PTPN6) (HUMAN) Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PTN6_HUMAN] Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. Publication Abstract from PubMed Protein tyrosine phosphatase (PTP) catalytic domains undergo a series of conformational changes in order to mediate dephosphorylation of their tyrosine phosphorylated substrates. An important conformational change occurs in the Tryptophan-Proline-Aspartic acid (WPD) loop, which contains the conserved catalytic aspartate. Upon substrate binding, the WPD loop transitions from the 'open' to the 'closed' state, thus allowing optimal positioning of the catalytic aspartate for substrate dephosphorylation. The dynamics of WPD loop conformational changes have previously been studied for PTP1B, HePTP, and the bacterial phosphatase YopH, however, have not yet been comprehensively studied for the non-receptor tyrosine phosphatase SHP-1 (PTPN6). However, there is no characterization of the extent of WPD loop movement between open and fully closed states. To structurally describe the changes in WPD loop conformation, we have determined the 1.4 A crystal structure of the catalytic domain of SHP-1 in the Apo state and the 1.8 A crystal structure of the SHP-1 catalytic domain in complex with a phosphate ion. We provide structural analysis for the WPD loop closed state of SHP phosphatases and the conformational changes that occur upon WPD loop closure. SHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound states.,Alicea-Velazquez NL, Boggon TJ Protein Pept Lett. 2013 Mar 18. PMID:23514039 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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