HIGH-RESOLUTION SOLUTION STRUCTURE OF THE BETA-CHEMOKINE HMIP-1-BETA BY MULTIDIMENSIONAL NMR

被引:217
作者
LODI, PJ
GARRETT, DS
KUSZEWSKI, J
TSANG, MLS
WEATHERBEE, JA
LEONARD, WJ
GRONENBORN, AM
CLORE, GM
机构
[1] NIDDKD,CHEM PHYS LAB,BETHESDA,MD 20892
[2] R&D SYST INC,MINNEAPOLIS,MN 55413
[3] NHLBI,PULM & MOLEC IMMUNOL SECT,BETHESDA,MD 20892
关键词
D O I
10.1126/science.8134838
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of similar to 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interfaceis formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.
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页码:1762 / 1767
页数:6
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