Crystals of the complex between human growth hormone and the extracellular domain of its receptor.
Single crystals suitable for high-resolution diffraction studies have been grown of the human growth hormone (hGH) complexed to the extracellular domain of its cloned receptor from the human liver (hGHbp), using the technique of repeat seeding. The crystals are in space group P2(1)2(1)2, with a = 145.8 A, b = 68.6 A, c = 76.0 A, and diffract to at least 2.7 A resolution on a rotating anode X-ray source. Analysis of the composition of these crystals showed the stoichiometry of the complex to be hGH: (hGHbp)2. This finding, coupled with biochemical data on the complex in solution, indicates that the biologically significant dimerization of the growth hormone receptor is mediated through a single hormone molecule. Structure determination of the complex is currently being completed.
Ultsch
M
M
Department of Protein Engineering Genetech, Inc., South San Francisco, CA 94080.
de Vos
A M
AM
Kossiakoff
A A
AA
D003460:Crystallization; D013006:Growth Hormone / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D011986:Receptors, Somatotropin / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D014961:X-Ray Diffraction / Q000379:methods
D011986:Receptors, Somatotropin; D011994:Recombinant Proteins; D013006:Growth Hormone