2tcl: Difference between revisions

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[[Image:2tcl.~~jpg~~|left|200px]]

[[Image:2tcl.png|left|200px]]

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

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

~~==Overview==~~

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~~In rheumatoid and osteoarthritis~~, ~~degradation of articular cartilage is mediated by the matrix metalloproteinases collagenase~~, ~~stromelysin and gelatinase. The key event in this process is~~ the ~~cleavage of triple helical collagen by collagenase. We have determined~~ the ~~crystal structure of the catalytic domain of human recombinant fibroblast collagenase complexed with a synthetic inhibitor~~ at 2.~~2 A resolution~~. ~~The protein fold~~ is ~~similar to the amino termini of~~ the zinc endopeptidases astacin thermolysin and elastase despite a lack of primary sequence homology. The conformation of the bound inhibitor provides a molecular basis for the design of inhibitors of collagenase and other matrix metalloproteinases. Such inhibitors should be useful in the treatment of a variety of diseases including arthritis and cancer.

The line below this paragraph, {{ABSTRACT_PUBMED_7656013}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 7656013 is the PubMed ID number.

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==About this Structure==

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[[Category: Borkakoti, N.]]

[[Category: Winkler, F K.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 17~~:22:49 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:52:21 2008''

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-[[Image:2tcl.jpg|left|200px]]
+{{Seed}}
+[[Image:2tcl.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2tcl|  PDB=2tcl  |  SCENE=  }}
-'''STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR'''
+===STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR===
-==Overview==
+<!--
-In rheumatoid and osteoarthritis, degradation of articular cartilage is mediated by the matrix metalloproteinases collagenase, stromelysin and gelatinase. The key event in this process is the cleavage of triple helical collagen by collagenase. We have determined the crystal structure of the catalytic domain of human recombinant fibroblast collagenase complexed with a synthetic inhibitor at 2.2 A resolution. The protein fold is similar to the amino termini of the zinc endopeptidases astacin thermolysin and elastase despite a lack of primary sequence homology. The conformation of the bound inhibitor provides a molecular basis for the design of inhibitors of collagenase and other matrix metalloproteinases. Such inhibitors should be useful in the treatment of a variety of diseases including arthritis and cancer.
+The line below this paragraph, {{ABSTRACT_PUBMED_7656013}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7656013 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7656013}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Borkakoti, N.]]
 [[Category: Winkler, F K.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:22:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:52:21 2008''