1ck7
From Proteopedia
(New page: 200px<br /> <applet load="1ck7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ck7, resolution 2.8Å" /> '''GELATINASE A (FULL-L...) |
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| - | [[Image:1ck7.gif|left|200px]]<br /> | + | [[Image:1ck7.gif|left|200px]]<br /><applet load="1ck7" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ck7" size=" | + | |
caption="1ck7, resolution 2.8Å" /> | caption="1ck7, resolution 2.8Å" /> | ||
'''GELATINASE A (FULL-LENGTH)'''<br /> | '''GELATINASE A (FULL-LENGTH)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Matrix metalloproteinases (MMPs) catalyze extracellular matrix | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CK7 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 ZN, CA, CL, NA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1CK7 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=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CK7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: metalloproteinase]] | [[Category: metalloproteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:55 2008'' |
Revision as of 10:06, 21 February 2008
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GELATINASE A (FULL-LENGTH)
Contents |
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.
Disease
Known diseases associated with this structure: Osteolysis, idiopathic, Saudi type OMIM:[120360], Winchester syndrome OMIM:[120360]
About this Structure
1CK7 is a Single protein structure of sequence from Homo sapiens with , , , and as ligands. Active as Gelatinase A, with EC number 3.4.24.24 Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 12:06:55 2008
Categories: Gelatinase A | Homo sapiens | Single protein | Bergmann, U. | Isupov, M. | Lindqvist, Y. | Morgunova, E. | Schneider, G. | Tryggvason, K. | Tuuttila, A. | CA | CL | NA | SO4 | ZN | Full-length | Gelatinase a | Hydrolase (metalloprotease) | Metalloproteinase
