Evidence for Involvement of the Carboxy Terminus of Helix 1 of Growth Hormone in Receptor Binding: Use of Charge Reversal Mutagenesis to Account for Calcium Dependence of Binding and for Design of Higher Affinity Analogs-Reference-Cited by-同舟云学术

Evidence for Involvement of the Carboxy Terminus of Helix 1 of Growth Hormone in Receptor Binding: Use of Charge Reversal Mutagenesis to Account for Calcium Dependence of Binding and for Design of Higher Affinity Analogs

Published:1994-10-04 Issue:39 Volume:33 Page:11724-11733
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rowlinson Scott W.,Barnard Ross,Bastiras Stan,Robins Allan J.,Senn Carol,Wells Julian R. E.,Brinkworth Ross,Waters Michael J.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00205a008

Reference42 articles.

1. Three-dimensional structure of a genetically engineered variant of porcine growth hormone.

2. A strategy for optimizing charge reversal mutagenesis of ion pairs in hormone—receptor or enzyme—substrate complexes

3. Use of calcium dependence as a means to study the interaction between growth hormones and their binding proteins in rabbit liver

4. Monoclonal Antibodies to the Rabbit Liver Growth Hormone Receptor: Production and Characterization*

5. An electrostatic model for the interaction between growth hormone and its receptor involving chelation of Ca2+ to the human growth hormone molecule

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1. Acid Denaturation of Recombinant Porcine Growth Hormone: Formation and Self-Association of Folding Intermediates;Biochemistry;2000-09-08

2. Analysis of binding properties between 20 kDa human growth hormone (hGH) and hGH receptor (hGHR): the binding affinity for hGHR extracellular domain and mode of receptor dimerization;Journal of Molecular Endocrinology;1999-12-01

3. The Growth Hormone Receptor;Comprehensive Physiology;1999-12

4. Molecular recognition events involved in the activation of the growth hormone receptor by growth hormone;J MOL RECOGNIT;1999

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