The molecular dynamics of N- and C-terminal interactions during autoinhibition and activation of formin mDial

Steered molecular dynamics (SMD) was used to identify the interacting amino-acid residues on the surfaces of formin mDia1 domains for DID–DAD interactions, which is responsible for formin autoinhibition, and DID–Rho GTPase, which is responsible for formin activation. Ionic interactions between Glu17...

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Bibliographic Details
Published in:Biophysics (Oxford) 2015-05, Vol.60 (3), p.361-364
Main Authors: Orshanskiy, I. A., Popinako, A. V., Koromyslova, A. D., Volokh, O. I., Shaitan, K. V., Sokolova, O. S.
Format: Article
Language:English
Subjects:
Amino acids
Biological and Medical Physics
Biophysics
Molecular biology
Molecular Biophysics
Physics
Physics and Astronomy
Proteins
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Summary:Steered molecular dynamics (SMD) was used to identify the interacting amino-acid residues on the surfaces of formin mDia1 domains for DID–DAD interactions, which is responsible for formin autoinhibition, and DID–Rho GTPase, which is responsible for formin activation. Ionic interactions between Glu178 and Arg248 and hydrophobic interactions between a carbon atom of Thr175 and the aromatic ring of Phe247 were the most stable. The DID–Rho interaction was the strongest, being mediated by triple ionic interactions of positively charged Rho residues with a DID amino-acid triplet, which included two negatively charged residues with an uncharged one between them. The DID sites binding with Rho and DAD overlap in part, but different DID amino-acid residues are involved in DID interactions with different partners. Conformational changes potentially arising in the formin domains upon activation or inactivation are discussed.
ISSN:0006-3509
1555-6654
DOI:10.1134/S0006350915030136