1hlg
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(New page: 200px<br /> <applet load="1hlg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hlg, resolution 3.Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 15:13, 12 November 2007
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CRYSTAL STRUCTURE OF HUMAN GASTRIC LIPASE
Overview
Fat digestion in humans requires not only the classical pancreatic lipase, but also gastric lipase, which is stable and active despite the highly, acidic stomach environment. We report here the structure of recombinant, human gastric lipase at 3.0-A resolution, the first structure to be, described within the mammalian acid lipase family. This globular enzyme, (379 residues) consists of a core domain belonging to the alpha/beta, hydrolase-fold family and a "cap" domain, which is analogous to that, present in serine carboxypeptidases. It possesses a classical catalytic, triad (Ser-153, His-353, Asp-324) and an oxyanion hole (NH groups of, Gln-154 and Leu-67). Four N-glycosylation sites were identified on the, electron density maps. The catalytic serine is deeply buried under a, segment consisting of 30 residues, which can be defined as a lid and, belonging to the cap domain. The displacement of the lid is necessary for, the substrates to have access to Ser-153. A phosphonate inhibitor was, positioned in the active site that clearly suggests the location of the, hydrophobic substrate binding site. The lysosomal acid lipase was modeled, by homology, and possible explanations for some previously reported, mutations leading to the cholesterol ester storage disease are given based, on the present model.
About this Structure
1HLG is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest., Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C, J Biol Chem. 1999 Jun 11;274(24):16995-7002. PMID:10358049
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