1EL0

SOLUTION STRUCTURE OF THE HUMAN CC CHEMOKINE, I-309

Summary for 1EL0

• Entry DOI: 10.2210/pdb1el0/pdb
• Descriptor: I-309 (1 entity in total)
• Functional Keywords: chemokine fold, immune system
• Total number of polymer chains: 1
• Total formula weight: 8594.19

Authors

Keizer, D.W.,Crump, M.P.,Lee, T.W.,Slupsky, C.M.,Clark-Lewis, I.,Sykes, B.D. (deposition date: 2000-03-11, release date: 2000-09-01, Last modification date: 2022-02-16)

Primary citation

Keizer, D.W.,Crump, M.P.,Lee, T.W.,Slupsky, C.M.,Clark-Lewis, I.,Sykes, B.D.
Human CC chemokine I-309, structural consequences of the additional disulfide bond.
Biochemistry, 39:6053-6059, 2000

PubMed Abstract: 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.

PubMed: 10821677
DOI: 10.1021/bi000089l

Experimental method

SOLUTION NMR