Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1996-7-30
pubmed:abstractText
Sequence comparison of natural relaxins and the investigation of the structure function relationship of chemically synthesized relaxin analogs have been used to identify two arginine residues on the surface of the main helix of the B chain as hormone-receptor interaction site. This site is sensitive to structural changes, in particular the conformation of the A chain loop. Introducing the active site of relaxin into noncrossreacting structural analogs such as insulin and bombyxin required a four amino acid exchange. Both hybrid hormones bound to the anti-porcine relaxin antibody R6 with high affinity, and the insulin analog, with an additional C-terminal truncation of the B chain, crossreacted with rat relaxin-receptors.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1052-6781
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
63-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Introduction of relaxin properties into other hormones of insulin-like structure.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston 29425, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't