1el0: Difference between revisions
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</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=1el0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1el0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1el0 RCSB], [http://www.ebi.ac.uk/pdbsum/1el0 PDBsum]</span></td></tr> | </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=1el0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1el0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1el0 RCSB], [http://www.ebi.ac.uk/pdbsum/1el0 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CCL1_HUMAN CCL1_HUMAN]] Cytokine that is chemotactic for monocytes but not for neutrophils. Binds to CCR8.<ref>PMID:1557400</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 22:49, 25 December 2014
SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309
Structural highlights
Function[CCL1_HUMAN] Cytokine that is chemotactic for monocytes but not for neutrophils. Binds to CCR8.[1] 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 PubMedI-309 is a member of the CC subclass of chemokines and is one of only three human chemokines known to contain an additional, third disulfide bond. The three-dimensional solution structure of I-309 was determined by (1)H nuclear magnetic resonance spectroscopy and dynamic simulated annealing. The structure of I-309, which remains monomeric at high concentrations, was determined on the basis of 978 experimental restraints. The N-terminal region of I-309 was disordered, as has been previously observed for the CC chemokine eotaxin but not others such as MCP-1 and RANTES. This was followed in I-309 by a well-ordered region between residues 13 and 69 that consisted of a 3(10)-helix, a triple-stranded antiparallel beta-sheet, and finally a C-terminal alpha-helix. Root-mean-square deviations of 0.61 and 1.16 were observed for the backbone and heavy atoms, respectively. A comparison of I-309 to eotaxin and HCC-2 revealed a significant structural change in the C-terminal region of the protein. The alpha-helix normally present in chemokines was terminated early and was followed by a short section of extended strand. These changes were a direct result of the additional disulfide bond present in this protein. An examination of the I-309 structure will aid in an understanding of the specificity of this protein with its receptor, CCR8. Human CC chemokine I-309, structural consequences of the additional disulfide bond.,Keizer DW, Crump MP, Lee TW, Slupsky CM, Clark-Lewis I, Sykes BD Biochemistry. 2000 May 23;39(20):6053-9. PMID:10821677[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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