Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1978-06

AUTHORS

P. De Meyts, E. Van Obberghen, J. Roth, A. Wollmer, D. Brandenburg

ABSTRACT

Insulin binding to its receptor leads to negatively cooperative interactions among the receptor sites. Studies with 29 insulin analogues (animal insulins and proinsulin, insulin-like growth factor and chemically modified insulins) which vary 1,000-fold in their affinity for the receptor and in their biological potency, suggest that a discrete invariable region on the surface of the insulin monomer is responsible for including the negative cooperativity. This domain comprises some of the eight carboxy-terminal residues of the B-chain and the A21 asparagine. Burying of this 'cooperative site' in the dimerisation of insulin leads to a loss of negative cooperativity. A revised mapping of the insulin molecule is proposed, featuring distinct bioactive and cooperative sites. More... »

PAGES

504-509

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/273504a0

DOI

http://dx.doi.org/10.1038/273504a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011569019

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/661960


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