1mnc: Difference between revisions

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[[Image:1mnc.~~gif~~|left|200px]]

[[Image:1mnc.png|left|200px]]

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~~'''~~STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET~~'''~~

===STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_7656015}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7656015 is the PubMed ID number.

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==About this Structure==

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[[Category: Spurlino, J C.]]

[[Category: Stams, T.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ 3 01:27:06 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:27:22 2008''

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-[[Image:1mnc.gif|left|200px]]
+{{Seed}}
+[[Image:1mnc.png|left|200px]]
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 {{STRUCTURE_1mnc|  PDB=1mnc  |  SCENE=  }}
-'''STRUCTURE OF HUMAN NEUTROPHIL COLLAGENASE REVEALS LARGE S1' SPECIFICITY POCKET'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7656015}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7656015 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7656015}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Spurlino, J C.]]
 [[Category: Stams, T.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:27:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 00:27:22 2008''