1ck7: Difference between revisions
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|PDB= 1ck7 |SIZE=350|CAPTION= <scene name='initialview01'>1ck7</scene>, resolution 2.8Å | |PDB= 1ck7 |SIZE=350|CAPTION= <scene name='initialview01'>1ck7</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1ck7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ck7 OCA], [http://www.ebi.ac.uk/pdbsum/1ck7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ck7 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. | Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Tryggvason, K.]] | [[Category: Tryggvason, K.]] | ||
[[Category: Tuuttila, A.]] | [[Category: Tuuttila, A.]] | ||
[[Category: full-length]] | [[Category: full-length]] | ||
[[Category: gelatinase some]] | [[Category: gelatinase some]] | ||
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[[Category: metalloproteinase]] | [[Category: metalloproteinase]] | ||
''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 19:23:11 2008'' | ||
Revision as of 19:23, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Activity: | Gelatinase A, with EC number 3.4.24.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GELATINASE A (FULL-LENGTH)
OverviewOverview
Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.
About this StructureAbout this Structure
1CK7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed., Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K, Science. 1999 Jun 4;284(5420):1667-70. PMID:10356396
Page seeded by OCA on Sun Mar 30 19:23:11 2008