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(New page: 200px<br /> <applet load="1mmb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mmb, resolution 2.1&Aring;" /> '''COMPLEX OF BB94 WITH...)
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'''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8'''<br />
'''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8'''<br />
==Overview==
==Overview==
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Matrix metalloproteinases are a family of zinc endopeptidases involved in, tissue remodeling. They have been implicated in various disease processes, including metastasis, joint destruction, and neurodegeneration. Human, neutrophil collagenase (HNC, MMP-8) represents one of the three, "interstitial" collagenases that cleave triple-helical collagens types I, II, and III. Its 163-residue catalytic domain (Met80 to Gly242) has been, expressed in Escherichia coli and crystallized as a noncovalent complex, with the hydroxamate inhibitor batimastat. The crystal structure, refined, to 2.1 A, demonstrates that batimastat binds to the S1-S2' sites and, coordinates to the catalytic zinc in a bidentate manner via the hydroxyl, and carbonyl oxygens of the hydroxamate group. The batimastat-collagenase, complex is described in detail, and the activities of batimastat analogues, are discussed in the light of the protein-inhibitor interactions revealed, by the crystallography studies.
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Matrix metalloproteinases are a family of zinc endopeptidases involved in tissue remodeling. They have been implicated in various disease processes including metastasis, joint destruction, and neurodegeneration. Human neutrophil collagenase (HNC, MMP-8) represents one of the three "interstitial" collagenases that cleave triple-helical collagens types I, II, and III. Its 163-residue catalytic domain (Met80 to Gly242) has been expressed in Escherichia coli and crystallized as a noncovalent complex with the hydroxamate inhibitor batimastat. The crystal structure, refined to 2.1 A, demonstrates that batimastat binds to the S1-S2' sites and coordinates to the catalytic zinc in a bidentate manner via the hydroxyl and carbonyl oxygens of the hydroxamate group. The batimastat-collagenase complex is described in detail, and the activities of batimastat analogues are discussed in the light of the protein-inhibitor interactions revealed by the crystallography studies.
==About this Structure==
==About this Structure==
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1MMB 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 CA, ZN and BAT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MMB OCA].
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1MMB 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=CA:'>CA</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=BAT:'>BAT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMB OCA].
==Reference==
==Reference==
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[[Category: metzincins]]
[[Category: metzincins]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:13:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:45 2008''

Revision as of 11:56, 21 February 2008

Image:1mmb.gif

1mmb, resolution 2.1Å

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COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8

Overview

Matrix metalloproteinases are a family of zinc endopeptidases involved in tissue remodeling. They have been implicated in various disease processes including metastasis, joint destruction, and neurodegeneration. Human neutrophil collagenase (HNC, MMP-8) represents one of the three "interstitial" collagenases that cleave triple-helical collagens types I, II, and III. Its 163-residue catalytic domain (Met80 to Gly242) has been expressed in Escherichia coli and crystallized as a noncovalent complex with the hydroxamate inhibitor batimastat. The crystal structure, refined to 2.1 A, demonstrates that batimastat binds to the S1-S2' sites and coordinates to the catalytic zinc in a bidentate manner via the hydroxyl and carbonyl oxygens of the hydroxamate group. The batimastat-collagenase complex is described in detail, and the activities of batimastat analogues are discussed in the light of the protein-inhibitor interactions revealed by the crystallography studies.

About this Structure

1MMB is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Neutrophil collagenase, with EC number 3.4.24.34 Full crystallographic information is available from OCA.

Reference

Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor., Grams F, Crimmin M, Hinnes L, Huxley P, Pieper M, Tschesche H, Bode W, Biochemistry. 1995 Oct 31;34(43):14012-20. PMID:7577999

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