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J. Biochem, 1998, Vol. 123, No. 1 62-70
© 1998 Japanese Biochemical Society

research-article

Solution Structure of CINC/Gro Investigated by Heteronuclear NMR

Hiroyuki Hanzawa*, Hideyuki Haruyama*,1, Kiyoshi Konishi{dagger}, Kazuyoshi Watanabe{ddagger} and Susumu Tsurufuji{ddagger}

* Analytical and Metabolic Research Laboratories, Sankyo Co., Ltd. 2–58, Hiromachi 1-chome, Shinagawa-ku, Tokyo 140
{dagger} Department of Biochemistry, Toyama Medical and Pharmaceutical University Faculty of Medicine Sugitani, Toyama 930-01
{ddagger} Institute of Cytosignal Research, Inc., Hiromachi, Shinagawa-ku, Tokyo 140

1To whom correspondence should be addressed

Cytokine-induced neutrophil chemoattractant (CINC/Gro) is a chemotactic factor for neutrophils in the rat and a member of the CXC chemokine family. The refined three-dimensional structure of CINC/Gro was derived with the aid of heteronuclear magnetic resonance spectroscopy and a hybrid method of distance geometry and simulated annealing. The backbone atomic r.m.s. differences for 19 structures about the mean coordinates for residues 7 to 70 are 0.69±0.15 Å for the dimer and 0.56±0.13 Å for the monomer. The N terminal region containing an ELR sequence, an essential motif for chemotactic activity, is disordered in solution, as in other CXC chemokines. The dimer structure consists of a six-stranded anti-parallel ß sheet with two C-terminal {alpha} helices on the ß sheet. The overall dimer structure of CINC/Gro is similar to that of human MGSA, though the backbone r.m.s.d.s between CINC/Gro and the two MGSA structures were high (1.81 and 2.34 Å for the monomer) in spite of the high sequence homology (67%). The major difference resides in the relative position of the C-terminal {alpha} helix with respect to the ß sheet. This results in a difference of interhelical distances in the dimer: wider (15 Å) in CINC/Gro, as in IL-8, than in MGSA (11.7 and 10 Å).


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