Structural understanding of the allosteric conformational change of cyclic AMP receptor protein by cyclic AMP binding.
By Hyung-Sik Won, T. Yamazaki, Tae-Woo Lee, Mi-Kyung Yoon, Sang-Ho Park, Y. Kyōgoku, Bong-Jin Lee. 2000
56 citations recorded by the source corpus.
Subfields: Molecular Biology, Nutrition and Dietetics
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In Molecular Biology
- Yusuf Tutar
- Catherine L. Lawson
- Helen M. Berman
- David Swigon
- Charalampos G. Kalodimos
- Marco Tonelli
- E. Krol
- R. Ebright
Citations in the corpus
- Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, background): “DNA binding domain in its active conformation (11, 54, 66, 67).”
- Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein (2013, background): “The shift in the inter-domain hinge was first observed by a structural inspection at the secondary structure level by NMR [24].”
- Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, methodology): “The present crystal structure confirms that the D helix of apo CRP includes Leu134–Lys152, which is consistent with the D138L-CRP crystal structure (Sharma et al., 2009) and our previous NMR analysis (Won et al., 2000).”
- cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review (2008, background): “The results of NMR studies confirm that after ligand binding, helix F protrudes, although its size is the same for apo-CRP and CRP-(cAMP) 2 [Won et al., 2000].”
- Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, background): “In N-oxide sensing and denitrification transcription factor (DNR; effector NO), a member of the CAP/FNR superfamily for which a structure of the isolated effector-binding domain in the absence of effector is available (27), the C-helix and the intersubunit C-helix/C -helix coiled coil seem to be par”
- 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”