Evolution of allostery in the cyclic nucleotide binding module
2007

Evolution of Allostery in Cyclic Nucleotide Binding Domains

Sample size: 7696 publication Evidence: moderate

Author Information

Author(s): Kannan Natarajan, Wu Jian, Anand Ganesh S, Yooseph Shibu, Neuwald Andrew F, Venter J Craig, Taylor Susan S

Primary Institution: University of California, San Diego

Hypothesis

How have cyclic nucleotide binding (CNB) domains evolved to sense a variety of second messenger signals?

Conclusion

CNB domains have evolved as a scaffold to sense a wide variety of second messenger signals.

Supporting Evidence

  • CNB domains have undergone major sequence variation during evolution.
  • Statistical comparison reveals that key residues have co-evolved with others to regulate function.
  • The study identified nearly 7,700 CNB domain containing proteins classified into 30 distinct families.

Takeaway

This study looks at how certain proteins can change shape to respond to different signals in the body, like a key fitting into different locks.

Methodology

The study involved identifying and classifying CNB domains from genomic sequences and analyzing their evolutionary information.

Limitations

The study primarily focuses on sequence data and may not capture all functional aspects of CNB domains.

Digital Object Identifier (DOI)

10.1186/gb-2007-8-12-r264

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication