1pex
From Proteopedia
(New page: 200px<br /> <applet load="1pex" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pex, resolution 2.7Å" /> '''COLLAGENASE-3 (MMP-1...) |
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| - | [[Image:1pex.gif|left|200px]]<br /> | + | [[Image:1pex.gif|left|200px]]<br /><applet load="1pex" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1pex" size=" | + | |
caption="1pex, resolution 2.7Å" /> | caption="1pex, resolution 2.7Å" /> | ||
'''COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN'''<br /> | '''COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Collagenase-3 (MMP-13) is a matrix metalloproteinase involved in human | + | Collagenase-3 (MMP-13) is a matrix metalloproteinase involved in human breast cancer pathology and in arthritic processes. The crystal structure of its C-terminal haemopexin-like domain has been solved by molecular replacement and refined to an R-value of 0.195 using data to 2.7 A resolution. This structure reveals a disk-like shape. The chain is folded into a beta-propeller structure of pseudo 4-fold symmetry, with the four propeller blades arranged around a funnel-like tunnel. This central tunnel tube harbours four ions assigned as two calcium and two chloride ions. The C-terminal domain of collagenase-3 has a similar structure to the equivalent domain of gelatinase A and fibroblast collagenase 1; however, its detailed structure and surface charge pattern has a somewhat greater similarity to the latter, in agreement with the subgrouping of MMP-13 with the collagenase subfamily of MMPs. It is proposed that several small structural differences may act together to confer the characteristic binding and cleavage specificities of collagenases for triple-helical substrates, probably in co-operation with a fitting interdomain linker. |
==About this Structure== | ==About this Structure== | ||
| - | 1PEX 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 SO4, CL and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1PEX 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=SO4:'>SO4</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Gohlke, U.]] | [[Category: Gohlke, U.]] | ||
| - | [[Category: Gomis-Ruth, F | + | [[Category: Gomis-Ruth, F X.]] |
[[Category: Knauper, V.]] | [[Category: Knauper, V.]] | ||
[[Category: Lopez-Otin, C.]] | [[Category: Lopez-Otin, C.]] | ||
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[[Category: c-terminal hemopexin-like domain of matrix-metalloproteinase]] | [[Category: c-terminal hemopexin-like domain of matrix-metalloproteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:08 2008'' |
Revision as of 12:28, 21 February 2008
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COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN
Overview
Collagenase-3 (MMP-13) is a matrix metalloproteinase involved in human breast cancer pathology and in arthritic processes. The crystal structure of its C-terminal haemopexin-like domain has been solved by molecular replacement and refined to an R-value of 0.195 using data to 2.7 A resolution. This structure reveals a disk-like shape. The chain is folded into a beta-propeller structure of pseudo 4-fold symmetry, with the four propeller blades arranged around a funnel-like tunnel. This central tunnel tube harbours four ions assigned as two calcium and two chloride ions. The C-terminal domain of collagenase-3 has a similar structure to the equivalent domain of gelatinase A and fibroblast collagenase 1; however, its detailed structure and surface charge pattern has a somewhat greater similarity to the latter, in agreement with the subgrouping of MMP-13 with the collagenase subfamily of MMPs. It is proposed that several small structural differences may act together to confer the characteristic binding and cleavage specificities of collagenases for triple-helical substrates, probably in co-operation with a fitting interdomain linker.
About this Structure
1PEX is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain., Gomis-Ruth FX, Gohlke U, Betz M, Knauper V, Murphy G, Lopez-Otin C, Bode W, J Mol Biol. 1996 Dec 6;264(3):556-66. PMID:8969305
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