2nsm: Difference between revisions
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[[Image:2nsm.gif|left|200px]] | [[Image:2nsm.gif|left|200px]] | ||
'''Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain''' | {{Structure | ||
|PDB= 2nsm |SIZE=350|CAPTION= <scene name='initialview01'>2nsm</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of the human carboxypeptidase N (Kininase I) catalytic domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2NSM is a [ | 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== | ||
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:// | 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]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:50:36 2008'' | ||
Revision as of 18:50, 20 March 2008
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| , 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
OverviewOverview
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 StructureAbout this Structure
2NSM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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