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[[Image:1cgf.jpg|left|200px]]<br /><applet load="1cgf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1cgf, resolution 2.1&Aring;" />
'''CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF'''<br />


==Overview==
==CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF==
Collagenase is a member of the matrix metalloproteinase (MMP) family of, enzymes. Aberrant regulation of this family has been implicated in, pathologies such as arthritis and metastasis. Two crystal forms of the, catalytic (19-kDa) domain of human fibroblast collagenase have been, determined using collagenase complexed with a peptide-based inhibitor, (CPLX) as a starting model [Lovejoy et al. (1994) Science 263, 375]. The, first crystal form (CF1) contains one molecule in the asymmetric unit and, has been determined at 1.9-A resolution with an R factor of 19.8%. The, second crystal form (CF2) contains two molecules (A and B) in the, asymmetric unit and has been determined at 2.1-A resolution with an R, factor of 19.7%. The catalytic domain of collagenase is spherical with an, active site cleft that contains a ligated catalytic zinc ion. Collagenase, shares some structural homology with the bacterial zinc proteinase, thermolysin [Matthews et al. (1972) Nature, New Biol. 238, 37], and the, crayfish digestive peptidase, astacin [Bode et al. (1992) Nature 358, 164]. The amino terminus (Leu 102 to Gly 105) of CF1 and CF2 molecules A, and B differs from the conformation found in CPLX by bending away from the, molecule and interacting with the active site cleft of symmetry-related, molecules. In this alternative conformation, both the mainchain nitrogen, and carbonyl oxygen of Leu 102 ligate the symmetry-related catalytic zinc., Although there are structural differences in the active site clefts of, CF1, CF2, and CPLX, a number of complex-stabilizing interactions are, conserved. The structure of collagenase will be useful for developing, compounds that selectively inhibit individual members of the closely, related matrix metalloproteinase family.
<StructureSection load='1cgf' size='340' side='right'caption='[[1cgf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cgf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CGF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cgf OCA], [https://pdbe.org/1cgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cgf RCSB], [https://www.ebi.ac.uk/pdbsum/1cgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cgf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MMP1_HUMAN MMP1_HUMAN] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.<ref>PMID:1645757</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cg/1cgf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cgf ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120353 120353]]
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1CGF 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> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CGF OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself., Lovejoy B, Hassell AM, Luther MA, Weigl D, Jordan SR, Biochemistry. 1994 Jul 12;33(27):8207-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8031754 8031754]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Interstitial collagenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Hassell AM]]
[[Category: Hassell, A.M.]]
[[Category: Jordan SR]]
[[Category: Jordan, S.R.]]
[[Category: Lovejoy B]]
[[Category: Lovejoy, B.]]
[[Category: Luther MA]]
[[Category: Luther, M.A.]]
[[Category: Weigl D]]
[[Category: Weigl, D.]]
[[Category: CA]]
[[Category: ZN]]
[[Category: hydrolase (metalloprotease)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:35:46 2008''

Latest revision as of 09:42, 7 February 2024

CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELFCRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF

Structural highlights

1cgf is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MMP1_HUMAN Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Desrochers PE, Jeffrey JJ, Weiss SJ. Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity. J Clin Invest. 1991 Jun;87(6):2258-65. PMID:1645757 doi:http://dx.doi.org/10.1172/JCI115262

1cgf, resolution 2.10Å

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