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1rtg
From Proteopedia
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|PDB= 1rtg |SIZE=350|CAPTION= <scene name='initialview01'>1rtg</scene>, resolution 2.6Å | |PDB= 1rtg |SIZE=350|CAPTION= <scene name='initialview01'>1rtg</scene>, resolution 2.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Gelatinase_A Gelatinase A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.24 3.4.24.24] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rtg OCA], [http://www.ebi.ac.uk/pdbsum/1rtg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rtg RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2. | In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Osteolysis, idiopathic, Saudi type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120360 120360]], Winchester syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120360 120360]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Gohlke, U.]] | [[Category: Gohlke, U.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
[[Category: gelatinase]] | [[Category: gelatinase]] | ||
[[Category: matrix metallo proteinase (mmp)]] | [[Category: matrix metallo proteinase (mmp)]] | ||
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[[Category: metzincin]] | [[Category: metzincin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:32:42 2008'' |
Revision as of 20:32, 30 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Gelatinase A, with EC number 3.4.24.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2
Overview
In common with most other matrix metalloproteinases, gelatinase A has a non-catalytic C-terminal domain that displays sequence homology to haemopexin. Crystals of this domain were used by molecular replacement to solve its molecular structure at 2.6 A resolution, which was refined to an R value of 17.9%. This structure has a disc-like shape, with the chain folded into a beta-propeller structure that has pseudo four-fold symmetry. Although the topology and the side-chain arrangement are very similar to the equivalent domain of fibroblast collagenase, significant differences in surface charge and contouring are observable on 1 side of the gelatinase A disc. This difference might be a factor in allowing the gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.
About this Structure
1RTG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function., Gohlke U, Gomis-Ruth FX, Crabbe T, Murphy G, Docherty AJ, Bode W, FEBS Lett. 1996 Jan 8;378(2):126-30. PMID:8549817
Page seeded by OCA on Sun Mar 30 23:32:42 2008
