Literature DB >> 1762154

Crystals of the complex between human growth hormone and the extracellular domain of its receptor.

M Ultsch1, A M de Vos, A A Kossiakoff.   

Abstract

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.

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Year:  1991        PMID: 1762154     DOI: 10.1016/0022-2836(91)90578-t

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  12 in total

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9.  Subdomain 2, Not the Transmembrane Domain, Determines the Dimerization Partner of Growth Hormone Receptor and Prolactin Receptor.

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Review 10.  Nanomedicines in the treatment of acromegaly: focus on pegvisomant.

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