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Cited by 212

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

The cAMP binding domain: An ancient signaling module

Open access
Berman, Helen M., Ten Eyck, Lynn F., Goodsell, David S., Haste, Nina M., Kornev, Alexandr, Taylor, Susan S.·2005·Proceedings of the National Academy of Sciences

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.

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Crossref · 10.1073/pnas.0408579102

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Metadata

Authors
Berman, H. M., Ten Eyck, L. F., Goodsell, D. S., Haste, N. M., Kornev, A., & Taylor, S. S.
Venue
Proceedings of the National Academy of Sciences
Published
2004-12-23
Volume
102
Issue
1
Pages
45-50
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2167344126
Cited by
212
References
1
FWCI
3.72
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The cAMP binding domain: An ancient signaling module. https://app.cochat.ai/papers/10.1073/pnas.0408579102
The paper
Berman, H. M., Ten Eyck, L. F., Goodsell, D. S., Haste, N. M., Kornev, A., & Taylor, S. S. (2005). The cAMP binding domain: An ancient signaling module. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0408579102

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