1cgl: Difference between revisions

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

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

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~~'''~~STRUCTURE OF THE CATALYTIC DOMAIN OF FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR~~'''~~

===STRUCTURE OF THE CATALYTIC DOMAIN OF FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR===

~~==Overview==~~

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~~Collagenase is a zinc-dependent endoproteinase and is a member of~~ the ~~matrix metalloproteinase~~ (~~MMP) family of enzymes. The MMPs participate in connective tissue remodeling events and aberrant regulation has been associated with several pathologies~~. ~~The 2~~.~~4 angstrom resolution structure of the inhibited enzyme revealed that~~, ~~in addition to the catalytic zinc, there~~ is ~~a second zinc ion and a calcium ion which play a major role in stabilizing~~ the ~~tertiary structure of collagenase~~. ~~Despite scant sequence homology, collagenase shares structural homology with two other endoproteinases, bacterial thermolysin and crayfish astacin. The detailed description of protein~~-inhibitor interactions present in the structure will aid in the design of compounds that selectively inhibit individual members of the MMP family. Such inhibitors will be useful in examining the function of MMPs in pathological processes.

The line below this paragraph, {{ABSTRACT_PUBMED_8278810}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8278810 is the PubMed ID number.

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==About this Structure==

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[[Category: Weigl, D.]]

[[Category: Metalloprotease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:42:51 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:43:20 2008''

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-[[Image:1cgl.gif|left|200px]]
+{{Seed}}
+[[Image:1cgl.png|left|200px]]
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@@ Line 9: / Line 10: @@
 {{STRUCTURE_1cgl|  PDB=1cgl  |  SCENE=  }}
-'''STRUCTURE OF THE CATALYTIC DOMAIN OF FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR'''
+===STRUCTURE OF THE CATALYTIC DOMAIN OF FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR===
-==Overview==
+<!--
-Collagenase is a zinc-dependent endoproteinase and is a member of the matrix metalloproteinase (MMP) family of enzymes. The MMPs participate in connective tissue remodeling events and aberrant regulation has been associated with several pathologies. The 2.4 angstrom resolution structure of the inhibited enzyme revealed that, in addition to the catalytic zinc, there is a second zinc ion and a calcium ion which play a major role in stabilizing the tertiary structure of collagenase. Despite scant sequence homology, collagenase shares structural homology with two other endoproteinases, bacterial thermolysin and crayfish astacin. The detailed description of protein-inhibitor interactions present in the structure will aid in the design of compounds that selectively inhibit individual members of the MMP family. Such inhibitors will be useful in examining the function of MMPs in pathological processes.
+The line below this paragraph, {{ABSTRACT_PUBMED_8278810}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8278810 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8278810}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Weigl, D.]]
 [[Category: Metalloprotease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:42:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:43:20 2008''