Publication Date:
1991-11-08
Description:
Human growth hormone (hGH) forms a 1:2 complex with the extracellular domain of its receptor-binding protein (hGHbp) as studied by crystallization, size exclusion chromatography, calorimetry, and a previously undescribed fluorescence quenching assay. These and other experiments with protein engineered variants of hGH have led to the identification of the binding determinants for two distinct but adjacent sites on hGH for the hGHbp, and the data indicated that there are two overlapping binding sites on the hGHbp for hGH. Furthermore, the binding of hGH to the hGHbp occurred sequentially; a first hGHbp molecule bound to site 1 on hGH and then a second hGHbp bound to site 2. Hormone-induced receptor dimerization is proposed to be relevant to the signal transduction mechanism for the hGH receptor and other related cytokine receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, B C -- Ultsch, M -- De Vos, A M -- Mulkerrin, M G -- Clauser, K R -- Wells, J A -- New York, N.Y. -- Science. 1991 Nov 8;254(5033):821-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1948064" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Antibodies, Monoclonal
;
Binding Sites
;
Chromatography, Gel
;
Growth Hormone/*metabolism
;
Humans
;
Kinetics
;
Macromolecular Substances
;
Models, Structural
;
Molecular Sequence Data
;
Mutagenesis, Site-Directed
;
Protein Conformation
;
Receptors, Somatotropin/genetics/isolation & purification/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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