Dynamically driven protein allostery

By Nataliya Popovych, Shangjin Sun, R. Ebright, Charalampos G. Kalodimos. 2006

617 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. Martin Karplus
2. Qiang Cui

In Molecular Biology

1. Junseock Koh
2. H. Youn
3. Qiang Cui
4. G. Roberts
5. M. Bott
6. Martin Karplus
7. Yusuf Tutar
8. Alfred Pühler

In Spectroscopy

1. Martin Karplus
2. Qiang Cui

Citations in the corpus

• Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, background): “These dynamics can underlie the entropy-driven CRP allostery that was previously observed (Popovych et al., 2006; Tzeng & Kalodimos, 2012), i.e. a dynamic conformational exchange is implicit in the considerable motional flexibility, particularly on the microsecond to millisecond time scale, of the…”
• Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein (2013, background): “The cooperative residue fluctuations may allow the propagation of the allosteric signal with the minimal structural changes in the mean conformation [45–48].”
• Allostery and cooperativity revisited (2008, methodology): “Although the analysis by Popovych et al. (2006) is suggestive, it does not prove that the origin of the negative cooperativity is the quenching of motion, or better, the reduction in configuration entropy, in (c-AMP)2–CAP N versus cAMP-CAPN.”
• 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 ”
• The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors (2014, result): “The proposed dynamic changes have been supported by a number of elegant NMR experiments [25, 29, 30] as well as coarse-grain modeling studies [31–33].”