1bo0: Difference between revisions

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[[Image:1bo0.jpg|left|200px]]
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{{STRUCTURE_1bo0|  PDB=1bo0  |  SCENE=  }}
'''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]]' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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>
== 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 ==
[[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/bo/1bo0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1bo0 ConSurf].
<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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1BO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BO0 OCA].
</div>
<div class="pdbe-citations 1bo0" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/8898111 8898111]
*[[Monocyte chemoattractant protein|Monocyte chemoattractant protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kim, K S.]]
[[Category: Kim K-S]]
[[Category: Kwon, D.]]
[[Category: Kwon D]]
[[Category: Lee, D.]]
[[Category: Lee D]]
[[Category: Sykes, B D.]]
[[Category: Sykes BD]]
[[Category: Chemotactic cytokine]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:45:08 2008''

Latest revision as of 09:26, 30 October 2024

MONOCYTE CHEMOATTRACTANT PROTEIN-3, NMR, MINIMIZED AVERAGE STRUCTUREMONOCYTE CHEMOATTRACTANT PROTEIN-3, NMR, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1bo0 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 1 model
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Kim KS, Rajarathnam K, Clark-Lewis I, Sykes BD. Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3. FEBS Lett. 1996 Oct 21;395(2-3):277-82. PMID:8898111
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