1mnc
From Proteopedia
(New page: 200px<br /> <applet load="1mnc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mnc, resolution 2.1Å" /> '''STRUCTURE OF HUMAN N...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mnc.gif|left|200px]]<br /> | + | [[Image:1mnc.gif|left|200px]]<br /><applet load="1mnc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mnc" size=" | + | |
caption="1mnc, resolution 2.1Å" /> | caption="1mnc, resolution 2.1Å" /> | ||
'''STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET'''<br /> | '''STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the catalytic domain of human neutrophil | + | The crystal structure of the catalytic domain of human neutrophil collagenase complexed with a peptide transition state analogue has been determined to a resolution of 2.1 A. The structure of the neutrophil enzyme, when compared with the three dimensional structure of the corresponding human fibroblast collagenase, shows differences in the first, S1', of the three enzyme specificity subsites on the carboxy-terminal side of the substrate scissile bond. The S1' pocket in the neutrophil collagenase is significantly larger than the equivalent site in the fibroblast enzyme, suggesting that the former enzyme has a broader range of possible substrates. Such differences also suggest approaches for the design of selective matrix metalloproteinase inhibitors. |
==About this Structure== | ==About this Structure== | ||
| - | 1MNC 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 ZN, CA and PLH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] Full crystallographic information is available from [http:// | + | 1MNC 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=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PLH:'>PLH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNC OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Rubin, B.]] | [[Category: Rubin, B.]] | ||
| - | [[Category: Smith, D | + | [[Category: Smith, D L.]] |
| - | [[Category: Spurlino, J | + | [[Category: Spurlino, J C.]] |
[[Category: Stams, T.]] | [[Category: Stams, T.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
| Line 24: | Line 23: | ||
[[Category: hydrolase (metalloprotease)]] | [[Category: hydrolase (metalloprotease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:10 2008'' |
Revision as of 11:57, 21 February 2008
|
STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET
Overview
The crystal structure of the catalytic domain of human neutrophil collagenase complexed with a peptide transition state analogue has been determined to a resolution of 2.1 A. The structure of the neutrophil enzyme, when compared with the three dimensional structure of the corresponding human fibroblast collagenase, shows differences in the first, S1', of the three enzyme specificity subsites on the carboxy-terminal side of the substrate scissile bond. The S1' pocket in the neutrophil collagenase is significantly larger than the equivalent site in the fibroblast enzyme, suggesting that the former enzyme has a broader range of possible substrates. Such differences also suggest approaches for the design of selective matrix metalloproteinase inhibitors.
About this Structure
1MNC is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Full crystallographic information is available from OCA.
Reference
Structure of human neutrophil collagenase reveals large S1' specificity pocket., Stams T, Spurlino JC, Smith DL, Wahl RC, Ho TF, Qoronfleh MW, Banks TM, Rubin B, Nat Struct Biol. 1994 Feb;1(2):119-23. PMID:7656015
Page seeded by OCA on Thu Feb 21 13:57:10 2008
