Comparing binding site information to binding affinity reveals that Crp/DNA complexes have several distinct binding conformers.

Abstract:

:We show that the cAMP receptor protein (Crp) binds to DNA as several different conformers. This situation has precluded discovering a high correlation between any sequence property and binding affinity for proteins that bend DNA. Experimentally quantified affinities of Synechocystis sp. PCC 6803 cAMP receptor protein (SyCrp1), the Escherichia coli Crp (EcCrp, also CAP) and DNA were analyzed to mathematically describe, and make human-readable, the relationship of DNA sequence and binding affinity in a given system. Here, sequence logos and weight matrices were built to model SyCrp1 binding sequences. Comparing the weight matrix model to binding affinity revealed several distinct binding conformations. These Crp/DNA conformations were asymmetrical (non-palindromic).

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Holmquist PC,Holmquist GP,Summers ML

doi

10.1093/nar/gkr369

subject

Has Abstract

pub_date

2011-08-01 00:00:00

pages

6813-24

issue

15

eissn

0305-1048

issn

1362-4962

pii

gkr369

journal_volume

39

pub_type

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