1sln
From Proteopedia
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| - | [[Image:1sln.gif|left|200px]] | + | [[Image:1sln.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842''' | + | {{Structure |
| + | |PDB= 1sln |SIZE=350|CAPTION= <scene name='initialview01'>1sln</scene>, resolution 2.27Å | ||
| + | |SITE= <scene name='pdbsite=CA1:Ca1+Are+The+Ligands+Of+Ca+Ion+Ca+259'>CA1</scene>, <scene name='pdbsite=CA2:Ca2+Are+The+Ligands+Of+Ca+Ion+Ca+260'>CA2</scene>, <scene name='pdbsite=CA3:Ca3+Are+The+Ligands+Of+Ca+Ion+Ca+261'>CA3</scene>, <scene name='pdbsite=INH:Site+Inh+Is+The+Binding+Site+For+The+N-Carboxy-Alkyl+Inh+...'>INH</scene>, <scene name='pdbsite=ZN1:Zn1+Are+The+Ligands+Of+Catalytic+(Zn+257)+Zn+Ion'>ZN1</scene> and <scene name='pdbsite=ZN2:Zn2+Are+The+Ligands+Of+Structural+(Zn+258)+Zn+Ion'>ZN2</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=INH:N-(R-CARBOXY-ETHYL)-ALPHA-(S)-(2-PHENYLETHYL)GLYCYL-L-ARGININE-N-PHENYLAMIDE'>INH</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SLN is a [ | + | 1SLN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLN OCA]. |
==Reference== | ==Reference== | ||
| - | Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme., Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD, et al., Protein Sci. 1995 Oct;4(10):1966-76. PMID:[http:// | + | Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme., Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD, et al., Protein Sci. 1995 Oct;4(10):1966-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8535233 8535233] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:06:38 2008'' |
Revision as of 12:06, 20 March 2008
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| , resolution 2.27Å | |||||||
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| Sites: | , , , , and | ||||||
| Ligands: | , and | ||||||
| Activity: | Stromelysin 1, with EC number 3.4.24.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842
Contents |
Overview
The proteolytic enzyme stromelysin-1 is a member of the family of matrix metalloproteinases and is believed to play a role in pathological conditions such as arthritis and tumor invasion. Stromelysin-1 is synthesized as a pro-enzyme that is activated by removal of an N-terminal prodomain. The active enzyme contains a catalytic domain and a C-terminal hemopexin domain believed to participate in macromolecular substrate recognition. We have determined the three-dimensional structures of both a C-truncated form of the proenzyme and an inhibited complex of the catalytic domain by X-ray diffraction analysis. The catalytic core is very similar in the two forms and is similar to the homologous domain in fibroblast and neutrophil collagenases, as well as to the stromelysin structure determined by NMR. The prodomain is a separate folding unit containing three alpha-helices and an extended peptide that lies in the active site of the enzyme. Surprisingly, the amino-to-carboxyl direction of this peptide chain is opposite to that adopted by the inhibitor and by previously reported inhibitors of collagenase. Comparison of the active site of stromelysin with that of thermolysin reveals that most of the residues proposed to play significant roles in the enzymatic mechanism of thermolysin have equivalents in stromelysin, but that three residues implicated in the catalytic mechanism of thermolysin are not represented in stromelysin.
Disease
Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]
About this Structure
1SLN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme., Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD, et al., Protein Sci. 1995 Oct;4(10):1966-76. PMID:8535233
Page seeded by OCA on Thu Mar 20 14:06:38 2008
Categories: Homo sapiens | Single protein | Stromelysin 1 | Becker, J W. | CA | INH | ZN | Collagen degradation | Fibroblast | Hydrolase | Metalloprotease
