A. M. de Vos investigated how growth hormone binds its growth hormone receptor. With colleagues, de Vos determined the X-ray crystallography structure of a complex containing human growth hormone and the extracellular portion of its receptor. The 1992 structure, measured at , contained one hormone molecule and two receptor molecules.[ref]
The growth hormone molecule contacted the two receptors through different binding surfaces, although the receptors used largely the same residues in each contact. Additional contact between the two receptors supported a model in which hormone binding brings a receptor pair together. This made the geometry of signal transduction concrete: a single bound hormone can organize more than one receptor molecule. The measured complex contained extracellular fragments, so the structure did not by itself record the complete activation process across a cell membrane.[ref]
Human growth hormone and extracellular domain of its receptor: crystal structure of the complex by A. M. de Vos and others. Abstract; distinct hormone-binding interfaces, receptor contacts and proposed sequential dimerization
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