Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 102, Issue 1, Pages 45-50Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0408579102
Keywords
allostery; conserved cyclic nucleoticle-binding motif
Categories
Funding
- NIDDK NIH HHS [P01 DK054441, DK 54441] Funding Source: Medline
- NIGMS NIH HHS [GM 34921, R01 GM034921, GM 21589, R01 GM021589] Funding Source: Medline
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available