2nsm

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[[Image:2nsm.gif|left|200px]]
[[Image:2nsm.gif|left|200px]]
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{{Structure
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|PDB= 2nsm |SIZE=350|CAPTION= <scene name='initialview01'>2nsm</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_2nsm", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysine_carboxypeptidase Lysine carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.3 3.4.17.3] </span>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2nsm| PDB=2nsm | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nsm OCA], [http://www.ebi.ac.uk/pdbsum/2nsm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nsm RCSB]</span>
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'''Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain'''
'''Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain'''
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[[Category: Tan, F.]]
[[Category: Tan, F.]]
[[Category: Than, M.]]
[[Category: Than, M.]]
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[[Category: caroxypeptidase]]
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[[Category: Caroxypeptidase]]
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[[Category: hormone processing]]
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[[Category: Hormone processing]]
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[[Category: peptide modification]]
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[[Category: Peptide modification]]
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[[Category: transthyretin-like domain]]
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[[Category: Transthyretin-like domain]]
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[[Category: zinc peptidase]]
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[[Category: Zinc peptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:51:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:07:44 2008''
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Revision as of 06:51, 4 May 2008

Image:2nsm.gif

Template:STRUCTURE 2nsm

Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain


Overview

Human carboxypeptidase N (CPN), a member of the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, is an extracellular glycoprotein synthesized in the liver and secreted into the blood, where it controls the activity of vasoactive peptide hormones, growth factors and cytokines by specifically removing C-terminal basic residues. Normally, CPN circulates in blood plasma as a hetero-tetramer consisting of two 83 kDa (CPN2) domains each flanked by a 48 to 55 kDa catalytic (CPN1) domain. We have prepared and crystallized the recombinant C-terminally truncated catalytic domain of human CPN1, and have determined and refined its 2.1 A crystal structure. The structural analysis reveals that CPN1 has a pear-like shape, consisting of a 319 residue N-terminal catalytic domain and an abutting, cylindrically shaped 79 residue C-terminal beta-sandwich transthyretin (TT) domain, more resembling CPD-2 than CPM. Like these other CPN/E members, two surface loops surrounding the active-site groove restrict access to the catalytic center, offering an explanation for why some larger protein carboxypeptidase inhibitors do not inhibit CPN. Modeling of the Pro-Phe-Arg C-terminal end of the natural substrate bradykinin into the active site shows that the S1' pocket of CPN1 might better accommodate P1'-Lys than Arg residues, in agreement with CPN's preference for cleaving off C-terminal Lys residues. Three Thr residues at the distal TT edge of CPN1 are O-linked to N-acetyl glucosamine sugars; equivalent sites in the membrane-anchored CPM are occupied by basic residues probably involved in membrane interaction. In tetrameric CPN, each CPN1 subunit might interact with the central leucine-rich repeat tandem of the cognate CPN2 subunit via a unique hydrophobic surface patch wrapping around the catalytic domain-TT interface, exposing the two active centers.

About this Structure

2NSM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain., Keil C, Maskos K, Than M, Hoopes JT, Huber R, Tan F, Deddish PA, Erdos EG, Skidgel RA, Bode W, J Mol Biol. 2007 Feb 16;366(2):504-16. Epub 2006 Nov 11. PMID:17157876 Page seeded by OCA on Sun May 4 09:51:42 2008

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