Linked Life Data

20158183

Source:http://linkedlifedata.com/resource/pubmed/id/20158183

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-3-4
pubmed:abstractText
Insulin initiates metabolic control by binding to the insulin receptor (IR) on target cells. Kinetic and mutational analyses have revealed two binding sites on the insulin molecule and the residues that compose them. However, direct determination of the insulin-IR interface is required to distinguish those residues that contribute to receptor binding from those required for structural stability. Here, we successfully characterized one binding site using the nuclear magnetic resonance (NMR) transferred cross-saturation method, which can directly determine the binding interface of a large protein-protein complex. The results showed that this binding site contained three residues that have not been identified previously by mutational analyses. On the basis of the structure of the contact site, we also identified a molecule that can displace insulin from the IR. In addition, we discuss the mode of interaction between insulin and its receptor relative to the NMR analyses.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1520-4804
pubmed:author
pubmed:issnType
Electronic
pubmed:day
11
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1917-22
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Direct determination of the insulin-insulin receptor interface using transferred cross-saturation experiments.
pubmed:affiliation
The Institute of Life Sciences, Ajinomoto Co Inc, 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki, Kanagawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't