ArticleBiophysical journal2006
The open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Arabidopsis plants deficient in constitutive class profilins reveal independent and quantitative genetic effects.BMC plant biology · 2015Article
- Nucleotide regulation of the structure and dynamics of G-actin.Biophysical journal · 2014Article
- ATP and ADP actin states.Biopolymers · 2013Article
- Structural basis for profilin-mediated actin nucleotide exchange.Journal of molecular biology · 2012Article
- The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin.Biophysical journal · 2009Article
- Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Control of the ability of profilin to bind and facilitate nucleotide exchange from G-actin.The Journal of biological chemistry · 2008Article
- Nucleotide-mediated conformational changes of monomeric actin and Arp3 studied by molecular dynamics simulations.Journal of molecular biology · 2008Article
- The structural determinants of macrolide-actin binding: in silico insights.Biophysical journal · 2007Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The open nucleotide pocket conformation of actin in the profilin:actinCaATP x-ray structure has been hypothesized to be a crucial intermediate for nucleotide exchange in the actin depolymerization/polymerization cycle. The requirement for ancillary modification of actin for crystallization leads to ambiguities in this interpretation, however. We have used molecular dynamics simulations to model the thermodynamic properties of the actin x-ray structure, outside the crystal lattice, in an aqueous environment with profilin removed. Our simulations show that the open-nucleotide-pocket, profilin-free structure is actually unstable, and closes. The coordination of actin to the nucleotide in the molecular-dynamics-derived closed structure is virtually identical to that in the closed profilin:actinSrATP x-ray structure. Thus, there is currently no thermodynamically stable structure representing the open-nucleotide-pocket state of actin.
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Registered trials
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