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Sticht, Heinrich ; Escher, Sylvia E. ; Schweimer, Kristian ; Forssmann, Wolf-Georg ; Rösch, Paul ; Adermann, Knut:
Solution structure of the human CC chemokine 2 : A monomeric representative of the CC chemokine subtype.
In: Biochemistry.
Bd. 38
(1999)
Heft 19
.
- S. 5995-6002.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi990065i
Abstract
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.