1HUM

SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER

Summary for 1HUM

• Entry DOI: 10.2210/pdb1hum/pdb
• Descriptor: HUMAN MACROPHAGE INFLAMMATORY PROTEIN 1 BETA (2 entities in total)
• Functional Keywords: cytokine(chemotactic)
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 15649.48

Authors

Clore, G.M.,Lodi, P.J.,Garrett, D.S.,Gronenborn, A.M. (deposition date: 1994-01-31, release date: 1994-04-30, Last modification date: 2024-10-23)

Primary citation

Lodi, P.J.,Garrett, D.S.,Kuszewski, J.,Tsang, M.L.,Weatherbee, J.A.,Leonard, W.J.,Gronenborn, A.M.,Clore, G.M.
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science, 263:1762-1767, 1994

PubMed Abstract: 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 approximately 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 interface is 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.

PubMed: 8134838

Experimental method

SOLUTION NMR