3u0v

Crystal Structure Analysis of human LYPLAL1

spinqualitylabelsall models 3u0v, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3u0v 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 1.72Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LYPL1_HUMAN Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site. Publication Abstract from PubMed Sequence homology indicates the existence of three human cytosolic acyl protein thioesterases, including APT1 that is known to depalmitoylate H- and N-Ras. The lysophospholipase-like 1 (LYPLAL1) protein is predicted to be related to APT1 and might also function as a potential triacylglycerol lipase involved in obesity. However, its role remained unclear. The 1.7 A crystal structure of LYPLAL1 reveals a fold very similar to APT1, but features a shape of the active site that precludes binding of long-chain substrates. Biochemical data demonstrate that LYPLAL1 exhibits neither phospholipase nor triacylglycerol lipase activity, but rather accepts short-chain substrates. Furthermore, extensive screening efforts using chemical array technique revealed a first small molecule inhibitor of LYPLAL1. Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity in spite of close relationship to acyl protein thioesterases.,Burger M, Zimmermann TJ, Kondoh Y, Stege P, Watanabe N, Osada H, Waldmann H, Vetter IR J Lipid Res. 2011 Nov 3. PMID:22052940 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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