1hdk: Difference between revisions
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Revision as of 16:30, 30 October 2007
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CHARCOT-LEYDEN CRYSTAL PROTEIN- PCMBS COMPLEX
OverviewOverview
Charcot-Leyden crystal (CLC) protein, initially reported to possess weak, lysophospholipase activity, is still considered to be the eosinophil's, lysophospholipase, but it shows no sequence similarities to any known, lysophospholipases. In contrast, CLC protein has moderate sequence, similarity, conserved genomic organization, and near structural identity, to members of the galectin superfamily, and it has been designated, galectin-10. To definitively determine whether or not CLC protein is a, lysophospholipase, we reassessed its enzymatic activity in peripheral, blood eosinophils and an eosinophil myelocyte cell line (AML14.3D10)., Antibody affinity chromatography was used to fully deplete CLC protein, from eosinophil lysates. The CLC-depleted lysates retained their full, ... [(full description)]
About this StructureAbout this Structure
1HDK is a [Single protein] structure of sequence from [Homo sapiens] with PMB as [ligand]. Active as [Lysophospholipase], with EC number [3.1.1.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion., Ackerman SJ, Liu L, Kwatia MA, Savage MP, Leonidas DD, Swaminathan GJ, Acharya KR, J Biol Chem. 2002 Apr 26;277(17):14859-68. Epub 2002 Feb 7. PMID:11834744
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