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SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE HCC-2, NMR, 30 STRUCTURES

Overview

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.

About this Structure

2HCC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype., Sticht H, Escher SE, Schweimer K, Forssmann WG, Rosch P, Adermann K, Biochemistry. 1999 May 11;38(19):5995-6002. PMID:10320325

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