Literature DB >> 20841566

Signals: tinkering with domains.

Erich Bornberg-Bauer1.   

Abstract

Evolution reuses established modules. At the level of cell signaling, protein domains are used in many contexts to transfer different messages. A frequently occurring binding domain uses a structural scaffold to allow for sequence variation at critical sites without compromising structural stability. Even random mutations have a high chance of conferring a novel function, and only a small fraction of available sequence space is actually explored. Accordingly, current lab techniques allow us to infer evolutionary routes, exploring the possible and the attainable in terms of complex structure-function relationships.

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Year:  2010        PMID: 20841566     DOI: 10.1126/scisignal.3139pe31

Source DB:  PubMed          Journal:  Sci Signal        ISSN: 1945-0877            Impact factor:   8.192


  2 in total

Review 1.  The language of the protein universe.

Authors:  Andrea Scaiewicz; Michael Levitt
Journal:  Curr Opin Genet Dev       Date:  2015-11-03       Impact factor: 5.578

2.  A lack of peptide binding and decreased thermostability suggests that the CASKIN2 scaffolding protein SH3 domain may be vestigial.

Authors:  Jamie J Kwan; Logan W Donaldson
Journal:  BMC Struct Biol       Date:  2016-09-13
  2 in total

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