2veu

Crystal structure of protein tyrosine phosphatase 1B in complex with an isothiazolidinone-containing inhibitor

spinqualitylabelsall models 2veu, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2veu is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: IZ1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PTN1_HUMAN Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure-based design and synthesis of isothiazolidinone (IZD) inhibitors of PTP1B containing imidazoles and imidazolines and their modification to interact with the B site of PTP1B are described here. The X-ray crystal structures of 3I and 4I complexed with PTP1B were solved and revealed the inhibitors are interacting extensively with the B site of the enzyme. Isothiazolidinone inhibitors of PTP1B containing imidazoles and imidazolines.,Douty B, Wayland B, Ala PJ, Bower MJ, Pruitt J, Bostrom L, Wei M, Klabe R, Gonneville L, Wynn R, Burn TC, Liu PC, Combs AP, Yue EW Bioorg Med Chem Lett. 2008 Jan 1;18(1):66-71. Epub 2007 Nov 9. PMID:18037290 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tyrosine phosphatase 3D structures

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