This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 17: | Line 16: | ||
[[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.]] | ||
| Line 26: | Line 25: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 14:28:08 2008
