1hfc: Difference between revisions

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-[[Image:1hfc.gif|left|200px]]<br />
-<applet load="1hfc" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1hfc, resolution 1.5&Aring;" />
-'''1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE'''<br />
-==Overview==
+==1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE==
-The X-ray crystal structure of a 19 kDa active fragment of human, fibroblast collagenase has been determined by the multiple isomorphous, replacement method and refined at 1.56 A resolution to an R-factor of, 17.4%. The current structure includes a bound hydroxamate inhibitor, 88, waters and three metal atoms (two zincs and a calcium). The overall, topology of the enzyme, comprised of a five stranded beta-sheet and three, alpha-helices, is similar to the thermolysin-like metalloproteinases., There are some important differences between the collagenase and, thermolysin families of enzymes. The active site zinc ligands are all, histidines (His-218, His-222, and His-228). The presence of a second zinc, ion in a structural role is a unique feature of the matrix, metalloproteinases. The binding properties of the active site cleft are, more dependent on the main chain conformation of the enzyme (and, substrate) compared with thermolysin. A mechanism of action for peptide, cleavage similar to that of thermolysin is proposed for fibroblast, collagenase.
+<StructureSection load='1hfc' size='340' side='right'caption='[[1hfc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hfc]] is a 1 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=1HFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFC 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]] 1.5&#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=PLH:METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC+ACID'>PLH</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=1hfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfc OCA], [https://pdbe.org/1hfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfc RCSB], [https://www.ebi.ac.uk/pdbsum/1hfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfc 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/hf/1hfc_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=1hfc 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/>
-HFC 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 and PLH 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFC OCA].
+__TOC__
+</StructureSection>
-==Reference==
-.56 A structure of mature truncated human fibroblast collagenase., Spurlino JC, Smallwood AM, Carlton DD, Banks TM, Vavra KJ, Johnson JS, Cook ER, Falvo J, Wahl RC, Pulvino TA, et al., Proteins. 1994 Jun;19(2):98-109. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8090713 8090713]
 [[Category: Homo sapiens]]
-[[Category: Interstitial collagenase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Smith DL]]
-[[Category: Smith, D.L.]]
+[[Category: Spurlino JC]]
-[[Category: Spurlino, J.C.]]
-[[Category: CA]]
-[[Category: PLH]]
-[[Category: ZN]]
-[[Category: metalloprotease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:17:18 2007''