1uwy

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{{STRUCTURE_1uwy| PDB=1uwy | SCENE= }}
{{STRUCTURE_1uwy| PDB=1uwy | SCENE= }}
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'''CRYSTAL STRUCTURE OF HUMAN CARBOXYPEPTIDASE M'''
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===CRYSTAL STRUCTURE OF HUMAN CARBOXYPEPTIDASE M===
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==Overview==
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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 beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached. Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides. Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
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(as it appears on PubMed at http://www.pubmed.gov), where 15066430 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15066430}}
==About this Structure==
==About this Structure==
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[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:13:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:23:48 2008''

Revision as of 16:23, 28 July 2008

Image:1uwy.png

Template:STRUCTURE 1uwy

CRYSTAL STRUCTURE OF HUMAN CARBOXYPEPTIDASE M

Template:ABSTRACT PUBMED 15066430

About this Structure

1UWY is a Single protein structure of sequence from Homo sapiens. 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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