2004
DOI: 10.1002/bies.20151
|View full text |Cite
|
Sign up to set email alerts
|

Insulin and its receptor: structure, function and evolution

Abstract: I present here a personal perspective on more than three decades of research into the structural biology of the insulin-receptor interaction. The solution of the three-dimensional structure of insulin in 1969 provided a detailed understanding of the insulin surfaces involved in self-assembly. In subsequent years, hundreds of insulin analogues were prepared by insulin chemists and molecular biologists, with the goal of relating the structure to the biological function of the molecule. The design of methods for … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

5
281
0
9

Year Published

2007
2007
2024
2024

Publication Types

Select...
7
2

Relationship

0
9

Authors

Journals

citations
Cited by 285 publications
(295 citation statements)
references
References 72 publications
5
281
0
9
Order By: Relevance
“…Essential residues implicated in insulin binding to the IR include Gly-1, Gln-5, Tyr-19, and Asn-21 on the A chain and Tyr-16, Gly 23, Phe-24, Phe-25, and Tyr-26 (GFFY motif) on the B chain that together form the ''classical binding surface'' (Fig. 1 A) (2,(20)(21)(22). Other important residues include IleA2 and ValA3, which are likely exposed during binding to the IR, and LeuA13, ValB12, and LeuB17 that maintain secondary structure.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Essential residues implicated in insulin binding to the IR include Gly-1, Gln-5, Tyr-19, and Asn-21 on the A chain and Tyr-16, Gly 23, Phe-24, Phe-25, and Tyr-26 (GFFY motif) on the B chain that together form the ''classical binding surface'' (Fig. 1 A) (2,(20)(21)(22). Other important residues include IleA2 and ValA3, which are likely exposed during binding to the IR, and LeuA13, ValB12, and LeuB17 that maintain secondary structure.…”
Section: Resultsmentioning
confidence: 99%
“…endocrinology ͉ insect ͉ reproduction ͉ vector V ertebrates and invertebrates produce a diversity of insulin-like peptide (ILP) superfamily members distinguished by a shared structural motif (1)(2)(3). Most ILPs are expressed as prepropeptides that consist of four major domains (Pre, B, C, and A).…”
mentioning
confidence: 99%
“…1A) (1). Although the hormone functions as a Zn 2ϩ -free monomer in the bloodstream (2), it is stored in pancreatic ␤-cells as a Zn 2ϩ -stabilized hexamer (3). Such self-assembly is of overarching importance to stable pharmaceutical formulation.…”
Section: -Iodo-tyrmentioning
confidence: 99%
“…Generally, receptor tyrosine kinases are activated due to ligand-induced dimerization followed by autophosphorylation of intracellular catalytic domains (9,10). In the case of the insulin receptor minifamily, the receptor monomers are predimerized by disulfide bonds, and ligand binding induces a major conformational change that eventually results in the catalytic subunits approaching each other (11,12 disulfide-linked hydrophilic extracellular ␣-subunit and membrane-bound ␤-subunit with a phosphotyrosine kinase domain (13).…”
mentioning
confidence: 99%