Allosteric regulation of the cAMP receptor protein.

By J. G. Harman. 2001

252 citations recorded by the source corpus.

Subfields: Genetics, Microbiology, Molecular Biology

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Citations in the corpus

Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, background): “coli, values in the same range have been reported, the affinity for cAMP (10 mM) also being greater than that for cGMP, at 16 mM (9, 42).”
Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, background): “In particular, an NMR study of this mutant revealed cAMP-induced resonance shifts for Val49, Leu61, Leu73 and Leu124, which differed from those observed for cAMP binding to wild-type CRP (Harman, 2001; Lee et al., 1991).”
Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein (2013, background): “The hinge region appears to play a key role by modulating the interdomain interactions and stabilizing the altered domain movements leading to the transcriptional activation [2,14,20].”
Genomic mapping of cAMP receptor protein (CRPMt) in Mycobacterium tuberculosis: relation to transcriptional start sites and the role of CRPMt as a transcription factor (2014, background): “In addition to its possible role in CRPMt regulation (52), cAMP binds to other transcription factors (53) and has important allosteric effects on enzyme function (54).”
Dynamically driven protein allostery (2006, background): “1 online), which is also responsible for the dimerization of the protein, and a DNA-binding domain at the C terminu”
Catabolite activator protein: DNA binding and transcription activation. (2004, background): “Readers interested in cAMP binding by CAP and the cAMPmediated allosteric transition in CAP are referred to recent articles reporting structures of the cAMP-liganded state of CAP [4,5] and the unliganded state of the CAP homolog CooA [6], recent articles describing the effects of cAMP binding on the”
cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review (2008, background): “…devoid of cAMP; CRP-(cAMP) 2 , the form of protein that dominates in solutions with micromolar concentrations of the ligand and is responsible for transcription activation, and CRP-(cAMP) 4 , the form of protein that dominates in solutions with millimolar concentrations of cAMP [Harman, 2001].”
Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli (2008, background): “Nonetheless, we did not incorporate cooperativity between ligand-binding sites into our model for several reasons: (i) the data for WT CRP was well fitted by our equilibrium-shift model even without the factor of cooperativity, (ii) the cooperativity of D53S CRP is not necessarily identical to that ”
Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, background): “The cAMP-mediated allosteric transition in CAP is a textbook example of modulation of DNA-binding activity by small-molecule binding and has been the subject of extensive structural, biophysical, biochemical, and genetic analysis (4).”
Neglected role of cAMP receptor protein monomer (2011, background): “DNA [ 2 ]. From this K1 can also be estimated from Eq. 12 as 1 9 10 -6 M with dimer-DNA dissociation constant of 1 9 10 -9 M. The dimerization constant in this study is different than the literature values 10 9 –10 10 M -1 [14, 20,”