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Science 20 January 1995:
Vol. 267. no. 5196, pp. 383 - 386
DOI: 10.1126/science.7529940
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Articles

Science, Vol 267, Issue 5196, 383-386
Copyright © 1995 by American Association for the Advancement of Science

articles

A hot spot of binding energy in a hormone-receptor interface

T Clackson and JA Wells

Department of Protein Engineering, Genentech, South San Francisco, CA 94080.

The x-ray crystal structure of the complex between human growth hormone (hGH) and the extracellular domian of its first bound receptor (hGHbp) shows that about 30 side chains from each protein make contact. Individual replacement of contact residues in the hGHbp with alanine showed that a central hydrophobic region, dominated by two tryptophan residues, accounts for more than three-quarters of the binding free energy. This "functional epitope" is surrounded by less important contact residues that are generally hydrophilic and partially hydrated, so that the interface resembles a cross section through a globular protein. The functionally important residues on the hGHbp directly contact those on hGH. Thus, only a small and complementary set of contact residues maintains binding affinity, a property that may be general to protein-protein interfaces.


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Structure of the LDL Receptor Extracellular Domain at Endosomal pH.
G. Rudenko, L. Henry, K. Henderson, K. Ichtchenko, M. S. Brown, J. L. Goldstein, and J. Deisenhofer (2002)
Science 298, 2353-2358
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Complement C3b/C3d and Cell Surface Polyanions Are Recognized by Overlapping Binding Sites on the Most Carboxyl-Terminal Domain of Complement Factor H.
J. Hellwage, T. S. Jokiranta, M. A. Friese, T. U. Wolk, E. Kampen, P. F. Zipfel, and S. Meri (2002)
J. Immunol. 169, 6935-6944
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Residues of VP26 of Herpes Simplex Virus Type 1 That Are Required for Its Interaction with Capsids.
P. Desai, J.-C. Akpa, and S. Person (2002)
J. Virol. 77, 391-404
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Characterization of the Ikappa B-kinase NEMO Binding Domain.
M. J. May, R. B. Marienfeld, and S. Ghosh (2002)
J. Biol. Chem. 277, 45992-46000
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Dynamics-modulated Biological Activity of Transforming Growth Factor beta 3.
E. V. Bocharov, D. M. Korzhnev, M. J. J. Blommers, T. Arvinte, V. Yu. Orekhov, M. Billeter, and A. S. Arseniev (2002)
J. Biol. Chem. 277, 46273-46279
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