1mmb: Difference between revisions

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[[Image:1mmb.gif|left|200px]]<br />

[[Image:1mmb.gif|left|200px]]<br /><applet load="1mmb" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1mmb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1mmb, resolution 2.1Å" />

'''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8'''<br />

==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.

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 [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].

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==

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[[Category: metzincins]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 18~~:13:~~01 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:45 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1mmb.gif|left|200px]]<br />
+[[Image:1mmb.gif|left|200px]]<br /><applet load="1mmb" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1mmb" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1mmb, resolution 2.1&Aring;" />
 '''COMPLEX OF BB94 WITH THE CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-8'''<br />
 ==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.
+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==
-MMB 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].
+MMB 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==
@@ Line 25: / Line 24: @@
 [[Category: metzincins]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:13:01 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:45 2008''