✦ LIBER ✦

Structure and evolution of insulins: Implications for receptor binding

✍ Scribed by J. Murray-Rust; A. N. McLeod; T. L. Blundell; S. P. Wood

Publisher: John Wiley and Sons
Year: 1992
Tongue: English
Weight: 833 KB
Volume: 14
Category: Article
ISSN: 0265-9247
DOI: 10.1002/bies.950140507

No coin nor oath required. For personal study only.

✦ Synopsis

Insulin is a member of a family of hormones, growth factors and neuropeptides which are found in both vertebrates and invertebrates. A common 'insulin fold' is probably adopted by all family members. Although the specificities of receptor binding are different, there is a possibility of co-evolution of polypeptides and their receptors.

In trod u ct io n

Tn the years since 1955 when the amino acid sequence of insulin was determined by Sanger and co-workers(l?') our knowledge of insulin and related proteins has increased dramatically. We now have sequences of more than 80 insulins and insulin-related proteins as well as site-directed mutants and chemically modified insulins. There are structures in several oligomeric states defined in the crystals by X-ray analysic, and in solution by 2-dimensional nmr. The relationship between sequence variation and the role of parts of the structure in processing, stora e, transport and receptor

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