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

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

Content Provider	Springer Nature Link
Author	Orshanskiy, I. A. Popinako, A. V. Koromyslova, A. D. Volokh, O. I. Shaitan, K. V. Sokolova, O. S.
Copyright Year	2015
Abstract	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.
Starting Page	361
Ending Page	364
Page Count	4
File Format	PDF
ISSN	00063509
Journal	Biophysics
Volume Number	60
Issue Number	3
e-ISSN	15556654
Language	English
Publisher	Pleiades Publishing
Publisher Date	2015-08-15
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	actin-binding proteins formin molecular dynamics DID DAD Rho GTPase Biophysics and Biological Physics
Content Type	Text
Resource Type	Article
Subject	Biophysics

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