View source for 2hcc


==SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES==
<StructureSection load='2hcc' size='340' side='right'caption='[[2hcc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hcc]] 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=2HCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HCC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</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=2hcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hcc OCA], [https://pdbe.org/2hcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hcc RCSB], [https://www.ebi.ac.uk/pdbsum/2hcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hcc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCL15_HUMAN CCL15_HUMAN] Chemotactic factor that attracts T-cells and monocytes, but not neutrophils, eosinophils, or B-cells. Acts mainly via CC chemokine receptor CCR1. Also binds to CCR3. CCL15(22-92), CCL15(25-92) and CCL15(29-92) are more potent chemoattractants than the small-inducible cytokine A15.<ref>PMID:15905581</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/hc/2hcc_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=2hcc ConSurf].
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== Publication Abstract from PubMed ==
HCC-2, a 66-amino acid residue human CC chemokine, was reported to induce chemotaxis on monocytes, T-lymphocytes, and eosinophils. The three-dimensional structure of HCC-2 has been determined by 1H nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations on the basis of 871 experimental restraints. The structure is well-defined, exhibiting average root-mean-square deviations of 0.58 and 0.96 A for the backbone heavy atoms and all heavy atoms of residues 5-63, respectively. In contrast to most other chemokines, subtle structural differences impede dimer formation of HCC-2 in a concentration range of 0.1 microM to 2 mM. HCC-2, however, exhibits the same structural elements as the other chemokines, i.e., a triple-stranded antiparallel beta-sheet covered by an alpha-helix, showing that the chemokine fold is not influenced by quaternary interactions. Structural investigations with a HCC-2 mutant prove that a third additional disulfide bond present in wild-type HCC-2 is not necessary for maintaining the relative orientation of the helix and the beta-sheet.

Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.,Sticht H, Escher SE, Schweimer K, Forssmann WG, Rosch P, Adermann K Biochemistry. 1999 May 11;38(19):5995-6002. PMID:10320325<ref>PMID:10320325</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Adermann K]]
[[Category: Escher SE]]
[[Category: Forssmann WG]]
[[Category: Roesch P]]
[[Category: Schweimer K]]
[[Category: Sticht H]]