1el0

<StructureSection load='1el0' size='340' side='right'caption='[[1el0]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1el0]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EL0 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=1el0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1el0 OCA], [https://pdbe.org/1el0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1el0 RCSB], [https://www.ebi.ac.uk/pdbsum/1el0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1el0 ProSAT]</span></td></tr>

[[https://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>

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== Publication Abstract from PubMed ==

I-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<ref>PMID:10821677</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1el0" style="background-color:#fffaf0;"></div>

[[Category: Clark-Lewis, I]]

[[Category: Crump, M P]]

[[Category: Keizer, D W]]

[[Category: Lee, T W]]

[[Category: Slupsky, C M]]

[[Category: Sykes, B D]]

[[Category: Immune system]]