1kbc: Difference between revisions

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==Overview==

Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue, remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease., Human neutrophil collagenase represents one of the three interstitial, collagenases that cleave triple-helical collagen of type I, II and III., Its catalytic domain (residues Phe79-Gly242) has been heterologously, expressed in Escherichia coli and crystallized as a non-covalent complex, with the hydroxamate inhibitor BB-1909, which has distinct selectivity, against different MMP, in a crystal form. The crystal structure, refined, to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor, that binds to the S1'-S3' subsites and coordinates to the catalytic Zn2+, in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the, hydroxamate group in a similar manner to batimastat. The, collagenase/BB-1909 complex is described in detail and compared with the, collagenase/batimastat complex. These studies provide information on MMP, specificity and thus may assist the development of more-selective MMP, inhibitors.

Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease. Human neutrophil collagenase represents one of the three interstitial collagenases that cleave triple-helical collagen of type I, II and III. Its catalytic domain (residues Phe79-Gly242) has been heterologously expressed in Escherichia coli and crystallized as a non-covalent complex with the hydroxamate inhibitor BB-1909, which has distinct selectivity against different MMP, in a crystal form. The crystal structure, refined to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor that binds to the S1'-S3' subsites and coordinates to the catalytic Zn2+ in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the hydroxamate group in a similar manner to batimastat. The collagenase/BB-1909 complex is described in detail and compared with the collagenase/batimastat complex. These studies provide information on MMP specificity and thus may assist the development of more-selective MMP inhibitors.

==About this Structure==

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[[Category: Betz, M.]]

[[Category: Bode, W.]]

[[Category: Gomis-Rueth, F.X.]]

[[Category: Gomis-Rueth, F X.]]

[[Category: CA]]

[[Category: HLE]]

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[[Category: mmp-8]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue, remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease., Human neutrophil collagenase represents one of the three interstitial, collagenases that cleave triple-helical collagen of type I, II and III., Its catalytic domain (residues Phe79-Gly242) has been heterologously, expressed in Escherichia coli and crystallized as a non-covalent complex, with the hydroxamate inhibitor BB-1909, which has distinct selectivity, against different MMP, in a crystal form. The crystal structure, refined, to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor, that binds to the S1'-S3' subsites and coordinates to the catalytic Zn2+, in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the, hydroxamate group in a similar manner to batimastat. The, collagenase/BB-1909 complex is described in detail and compared with the, collagenase/batimastat complex. These studies provide information on MMP, specificity and thus may assist the development of more-selective MMP, inhibitors.
+Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease. Human neutrophil collagenase represents one of the three interstitial collagenases that cleave triple-helical collagen of type I, II and III. Its catalytic domain (residues Phe79-Gly242) has been heterologously expressed in Escherichia coli and crystallized as a non-covalent complex with the hydroxamate inhibitor BB-1909, which has distinct selectivity against different MMP, in a crystal form. The crystal structure, refined to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor that binds to the S1'-S3' subsites and coordinates to the catalytic Zn2+ in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the hydroxamate group in a similar manner to batimastat. The collagenase/BB-1909 complex is described in detail and compared with the collagenase/batimastat complex. These studies provide information on MMP specificity and thus may assist the development of more-selective MMP inhibitors.
 ==About this Structure==
@@ Line 16: / Line 16: @@
 [[Category: Betz, M.]]
 [[Category: Bode, W.]]
-[[Category: Gomis-Rueth, F.X.]]
+[[Category: Gomis-Rueth, F X.]]
 [[Category: CA]]
 [[Category: HLE]]
@@ Line 29: / Line 29: @@
 [[Category: mmp-8]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:12:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:10 2008''