1bo0
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
==MONOCYTE CHEMOATTRACTANT PROTEIN-3, NMR, MINIMIZED AVERAGE STRUCTURE== | ==MONOCYTE CHEMOATTRACTANT PROTEIN-3, NMR, MINIMIZED AVERAGE STRUCTURE== | ||
- | <StructureSection load='1bo0' size='340' side='right'caption='[[1bo0 | + | <StructureSection load='1bo0' size='340' side='right'caption='[[1bo0]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1bo0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1bo0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BO0 FirstGlance]. <br> |
- | </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=1bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bo0 OCA], [https://pdbe.org/1bo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bo0 RCSB], [https://www.ebi.ac.uk/pdbsum/1bo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bo0 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bo0 OCA], [https://pdbe.org/1bo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bo0 RCSB], [https://www.ebi.ac.uk/pdbsum/1bo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bo0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/CCL7_HUMAN CCL7_HUMAN] Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin. Binds to CCR1, CCR2 and CCR3. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 18: | Line 19: | ||
</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=1bo0 ConSurf]. | </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=1bo0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 1H-NMR spectroscopy and analytical ultracentrifugation studies reveal that monocyte chemoattractant protein-3 (MCP-3) is a monomer. NMR solution structure shows that MCP-3 adopts an alphabeta fold similar to what is observed in structures of other known chemokines. However, MCP-3 is unique in that it does not show a propensity to form dimers. The closely related chemokines MCP-1 and MCP-2 show a monomer-dimer equilibrium in sedimentation equilibrium studies (approximately 0.2-2 mg/ml). As these proteins are present at nanomolar concentrations in vivo, the results suggest that they are monomeric at functional concentrations and that the monomer is the functionally significant form of MCP-1, MCP-2 and MCP-3. | ||
- | |||
- | Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3.,Kim KS, Rajarathnam K, Clark-Lewis I, Sykes BD FEBS Lett. 1996 Oct 21;395(2-3):277-82. PMID:8898111<ref>PMID:8898111</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1bo0" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Monocyte chemoattractant protein|Monocyte chemoattractant protein]] | *[[Monocyte chemoattractant protein|Monocyte chemoattractant protein]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Kim | + | [[Category: Kim K-S]] |
- | [[Category: Kwon | + | [[Category: Kwon D]] |
- | [[Category: Lee | + | [[Category: Lee D]] |
- | [[Category: Sykes | + | [[Category: Sykes BD]] |
- | + | ||
- | + |
Revision as of 15:34, 13 March 2024
MONOCYTE CHEMOATTRACTANT PROTEIN-3, NMR, MINIMIZED AVERAGE STRUCTURE
|
Categories: Homo sapiens | Large Structures | Kim K-S | Kwon D | Lee D | Sykes BD