1slm: Difference between revisions

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[[Image:1slm.gif|left|200px]]<br />
[[Image:1slm.jpg|left|200px]]<br /><applet load="1slm" size="450" color="white" frame="true" align="right" spinBox="true"  
<applet load="1slm" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1slm, resolution 1.90&Aring;" />
caption="1slm, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF FIBROBLAST STROMELYSIN-1: THE C-TRUNCATED HUMAN PROENZYME'''<br />
'''CRYSTAL STRUCTURE OF FIBROBLAST STROMELYSIN-1: THE C-TRUNCATED HUMAN PROENZYME'''<br />
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==About this Structure==
==About this Structure==
1SLM 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 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Sites: CA1, CA2, ZN1 and ZN2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SLM OCA].  
1SLM 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 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <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=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>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SLM OCA].  


==Reference==
==Reference==
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[[Category: metalloprotease]]
[[Category: metalloprotease]]


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Revision as of 18:50, 18 December 2007

File:1slm.jpg


1slm, resolution 1.90Å

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CRYSTAL STRUCTURE OF FIBROBLAST STROMELYSIN-1: THE C-TRUNCATED HUMAN PROENZYME

OverviewOverview

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.

DiseaseDisease

Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]

About this StructureAbout this Structure

1SLM is a Single protein structure of sequence from Homo sapiens with ZN and CA as ligands. Active as Stromelysin 1, with EC number 3.4.24.17 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

ReferenceReference

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

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