1dok: Difference between revisions
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==MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM== | ==MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM== | ||
<StructureSection load='1dok' size='340' side='right' caption='[[1dok]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1dok' size='340' side='right' caption='[[1dok]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1dok]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DOK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dok]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DOK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dok OCA], [http://pdbe.org/1dok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dok RCSB], [http://www.ebi.ac.uk/pdbsum/1dok PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dok OCA], [http://pdbe.org/1dok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dok RCSB], [http://www.ebi.ac.uk/pdbsum/1dok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dok ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1dok_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/do/1dok_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[User:Coline Perrin/CCL2|User:Coline Perrin/CCL2]] | *[[User:Coline Perrin/CCL2|User:Coline Perrin/CCL2]] | ||
== References == | == References == | ||
Revision as of 10:47, 13 December 2017
MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORMMONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM
Structural highlights
Function[CCL2_HUMAN] Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe X-ray crystal structure of recombinant human monocyte chemoattractant protein (MCP-1) has been solved in two crystal forms. One crystal form (P), refined to 1.85 A resolution, contains a dimer in the asymmetric unit, while the other (I) contains a monomer and was refined at 2.4 A. Although both crystal forms grow together in the same droplet, the respective quaternary structures of the protein differ dramatically. In addition, both X-ray structures differ to a similar extent from the solution structure of MCP-1. Such extent of variability of quaternary structures is unprecedented. In the crystal structures, the well-ordered N termini of MCP-1 form 3(10)-helices. Comparison of the three MCP-1 structures revealed a direct correlation between the main-chain conformation of the first two cysteine residues and the quaternary arrangements. These data can be used to explain the structural basis for the assignment of residues responsible for biological activity. The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions.,Lubkowski J, Bujacz G, Boque L, Domaille PJ, Handel TM, Wlodawer A Nat Struct Biol. 1997 Jan;4(1):64-9. PMID:8989326[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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