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1f57

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[[Image:1f57.jpg|left|200px]]
[[Image:1f57.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1f57 |SIZE=350|CAPTION= <scene name='initialview01'>1f57</scene>, resolution 1.75&Aring;
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The line below this paragraph, containing "STRUCTURE_1f57", 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=DCY:D-CYSTEINE'>DCY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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/Carboxypeptidase_A Carboxypeptidase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.1 3.4.17.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1f57| PDB=1f57 | 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=1f57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f57 OCA], [http://www.ebi.ac.uk/pdbsum/1f57 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f57 RCSB]</span>
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}}
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'''CARBOXYPEPTIDASE A COMPLEX WITH D-CYSTEINE AT 1.75 A'''
'''CARBOXYPEPTIDASE A COMPLEX WITH D-CYSTEINE AT 1.75 A'''
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[[Category: Chong, C R.]]
[[Category: Chong, C R.]]
[[Category: Joshua-Tor, L.]]
[[Category: Joshua-Tor, L.]]
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[[Category: metalloprotease inhibitor]]
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[[Category: Metalloprotease inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:54:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:09 2008''
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Revision as of 12:54, 2 May 2008

Image:1f57.jpg

Template:STRUCTURE 1f57

CARBOXYPEPTIDASE A COMPLEX WITH D-CYSTEINE AT 1.75 A


Overview

D-Cysteine differs from the antiarthritis drug D-penicillamine by only two methyl groups on the beta-carbon yet inhibits carboxypeptidase A (CPD) by a distinct mechanism: D-cysteine binds tightly to the active site zinc, while D-penicillamine catalyzes metal removal. To investigate the structural basis for this difference, we solved the crystal structure of carboxypeptidase A complexed with D-cysteine (D-Cys) at 1.75-A resolution. D-Cys binds the active site zinc with a sulfur ligand and forms additional interactions with surrounding side chains of the enzyme. The structure explains the difference in potency between D-Cys and L-Cys and provides insight into the mechanism of D-penicillamine inhibition. D-Cys binding induces a concerted motion of the side chains around the zinc ion, similar to that found in other carboxypeptidase-inhibitor crystal structures and along a limited path. Analysis of concerted motions of CPD and CPD-inhibitor crystal structures reveals a clustering of these structures into distinct groups. Using the restricted conformational flexibility of a drug target in this type of analysis could greatly enhance efficiency in drug design.

About this Structure

1F57 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75 A - inhibitor-induced conformational changes., van Aalten DM, Chong CR, Joshua-Tor L, Biochemistry. 2000 Aug 22;39(33):10082-9. PMID:10955996 Page seeded by OCA on Fri May 2 15:54:54 2008

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