3shi: Difference between revisions

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<StructureSection load='3shi' size='340' side='right'caption='[[3shi]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3shi' size='340' side='right'caption='[[3shi]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3shi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHI FirstGlance]. <br>
<table><tr><td colspan='2'>[[3shi]] is a 3 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=3SHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHI FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cge|1cge]], [[1hfc|1hfc]], [[966c|966c]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP1, CLG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] </span></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=3shi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shi OCA], [https://pdbe.org/3shi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shi RCSB], [https://www.ebi.ac.uk/pdbsum/3shi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shi ProSAT]</span></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=3shi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shi OCA], [https://pdbe.org/3shi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shi RCSB], [https://www.ebi.ac.uk/pdbsum/3shi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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> 
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pseudocontact shifts (pcs) and paramagnetic residual dipolar couplings (rdc) provide structural information that can be used to assess the adequacy of a crystallographic structure to represent the solution structure of a protein. This can be done by attaching a lanthanide binding tag to the protein. There are cases in which only local rearrangements are sufficient to match the NMR data and cases where significant secondary structure or domain rearrangements from the solid state to the solution state are needed. We show that the two cases are easily distinguishable. Whereas the use of solution restraints in the latter case is described in the literature, here we deal with how to obtain a better model of the solution structure in a case (the catalytic domain of the matrix metalloproteinase MMP-1) of the former class.
 
The catalytic domain of MMP-1 studied through tagged lanthanides.,Bertini I, Calderone V, Cerofolini L, Fragai M, Geraldes CF, Hermann P, Luchinat C, Parigi G, Teixeira JM FEBS Lett. 2011 Sep 19. PMID:21945315<ref>PMID:21945315</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3shi" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Interstitial collagenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bertini, I]]
[[Category: Bertini I]]
[[Category: Calderone, V]]
[[Category: Calderone V]]
[[Category: Cerofolini, L]]
[[Category: Cerofolini L]]
[[Category: Fragai, M]]
[[Category: Fragai M]]
[[Category: Geraldes, C F.G C]]
[[Category: Geraldes CFGC]]
[[Category: Hermann, P]]
[[Category: Hermann P]]
[[Category: Luchinat, C]]
[[Category: Luchinat C]]
[[Category: Parigi, G]]
[[Category: Parigi G]]
[[Category: Teixeira, J]]
[[Category: Teixeira J]]
[[Category: Hydrolase]]
[[Category: Lanthanide]]
[[Category: Matrix metalloproteinase]]
[[Category: Paramagnetic restraint]]
[[Category: Paramagnetic tag]]
[[Category: Protein refinement]]
[[Category: Residual dipolar coupling]]

Latest revision as of 15:56, 14 March 2024

Crystal structure of human MMP1 catalytic domain at 2.2 A resolutionCrystal structure of human MMP1 catalytic domain at 2.2 A resolution

Structural highlights

3shi is a 3 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 2.2Å
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]

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

3shi, resolution 2.20Å

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OCA
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