2HCC

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

Summary for 2HCC

• Entry DOI: 10.2210/pdb2hcc/pdb
• Descriptor: HUMAN CHEMOKINE HCC-2 (1 entity in total)
• Functional Keywords: chemokine, human, hcc-2, mip-5, leukotactin-1, chemotaxis, cc-chemokine
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: Q16663
• Total number of polymer chains: 1
• Total formula weight: 7222.47

Authors

Sticht, H.,Escher, S.E.,Schweimer, K.,Forssmann, W.G.,Roesch, P.,Adermann, K. (deposition date: 1998-07-03, release date: 1999-07-13, Last modification date: 2022-03-09)

Primary citation

Sticht, H.,Escher, S.E.,Schweimer, K.,Forssmann, W.G.,Rosch, P.,Adermann, K.
Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
Biochemistry, 38:5995-6002, 1999

PubMed 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.

PubMed: 10320325
DOI: 10.1021/bi990065i

Experimental method

SOLUTION NMR