1uwy
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN CARBOXYPEPTIDASE M
Overview
Carboxypeptidase M (CPM), an extracellular, glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein, belonging to the CPN/E subfamily of "regulatory", metallo-carboxypeptidases, specifically removes C-terminal basic residues, from peptides and proteins. Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone, and growth factor activity at the cell surface, and in the, membrane-localized degradation of extracellular proteins. We have, crystallized human GPI-free CPM, and have determined and refined its 3.0A, crystal structure. The structure analysis reveals that CPM consists of a, 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but, only distantly related to CPA/B), an adjacent 86 residue ... [(full description)]
About this Structure
1UWY is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Active as [[1]], with EC number [3.4.17.12]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity., Reverter D, Maskos K, Tan F, Skidgel RA, Bode W, J Mol Biol. 2004 Apr 23;338(2):257-69. PMID:15066430
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