1ck7: Difference between revisions

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|PDB= 1ck7 |SIZE=350|CAPTION= <scene name='initialview01'>1ck7</scene>, resolution 2.8&Aring;
|PDB= 1ck7 |SIZE=350|CAPTION= <scene name='initialview01'>1ck7</scene>, resolution 2.8&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|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.
==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: Tryggvason, K.]]
[[Category: Tryggvason, K.]]
[[Category: Tuuttila, A.]]
[[Category: Tuuttila, A.]]
[[Category: CA]]
[[Category: CL]]
[[Category: NA]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: full-length]]
[[Category: full-length]]
[[Category: gelatinase some]]
[[Category: gelatinase some]]
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[[Category: metalloproteinase]]
[[Category: metalloproteinase]]


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