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The cAMP binding domain: An ancient signaling module

Academic Article
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Overview

authors

  • Berman, H. M.
  • Ten Eyck, L. F.
  • Goodsell, David
  • Haste, N. M.
  • Kornev, A.
  • Taylor, S. S.

publication date

  • January 2005

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • cAMP-binding domains from several different proteins were analyzed to determine the properties and interactions of this recognition motif. Systematic computational analyses, including structure-based sequence comparison, surface matching, affinity grid analysis, and analyses of the ligand protein interactions were carried out. These analyses show distinctive roles of the sugar phosphate and the adenine in the cAMP-binding module. We propose that the cAMP-binding regulatory proteins function by providing an allosteric system in which the presence or absence of cAMP produces a substantial structural change through the loss of hydrophobic interactions with the adenine ring and consequent repositioning of the C helix. The modified positioning of the helix in turn is recognized by a protein-binding event, completing the allostery.

subject areas

  • Amino Acid Sequence
  • Cyclic AMP
  • Databases, Protein
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Proteins
  • Sequence Alignment
  • Sequence Analysis, Protein
  • Signal Transduction
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Research

keywords

  • allostery
  • conserved cyclic nucleoticle-binding motif
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Identity

PubMed Central ID

  • PMC544069

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0408579102

PubMed ID

  • 15618393
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Additional Document Info

start page

  • 45

end page

  • 50

volume

  • 102

issue

  • 1

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