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1el0
From Proteopedia
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SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Asthma, susceptibility to OMIM:[601156], HIV1, resistance to OMIM:[601156]
About this Structure
1EL0 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 16:44:30 2007
