2h02 | pdb_00002h02
Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
Structural highlights
FunctionPTPRB_HUMAN Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin (By similarity).[1] [2] 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 PubMedThe sulfamic acid phosphotyrosine mimetic was coupled with a previously known malonate template to obtain highly selective and potent inhibitors of HPTPbeta. Potentially hydrolyzable malonate ester functionalities were replaced with 1,2,4-oxadiazoles without a significant effect on HPTPbeta potency. Design and synthesis of potent, non-peptidic inhibitors of HPTPbeta.,Amarasinghe KK, Evdokimov AG, Xu K, Clark CM, Maier MB, Srivastava A, Colson AO, Gerwe GS, Stake GE, Howard BW, Pokross ME, Gray JL, Peters KG Bioorg Med Chem Lett. 2006 Aug 15;16(16):4252-6. Epub 2006 Jun 12. PMID:16759857[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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