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2nsm

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[[Image:2nsm.gif|left|200px]]<br /><applet load="2nsm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2nsm.gif|left|200px]]
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caption="2nsm, resolution 2.1&Aring;" />
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'''Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain'''<br />
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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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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2NSM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NSM OCA].
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2NSM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NSM OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17157876 17157876]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17157876 17157876]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysine carboxypeptidase]]
[[Category: Lysine carboxypeptidase]]
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[[Category: zinc peptidase]]
[[Category: zinc peptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:50:36 2008''

Revision as of 15:50, 20 March 2008

Image:2nsm.gif


PDB ID 2nsm

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: and
Activity: Lysine carboxypeptidase, with EC number 3.4.17.3
Coordinates: save as pdb, mmCIF, xml



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

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