From Proteopedia
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Function
Twinfilin (Twi) is an actin-monomer-binding protein which is composed of 2 Actin Depolimerizing Factor Homology (ADF-H) domains. Twi forms a 1:1 complex with ADP-actin-monomer, inhibits nucleotide exchange on actin monomers and prevents assembly of the monomer to filaments[1].
Disease
Relevance
Structural highlights
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3D structures of twifilin
Updated on 31-December-2018
Domains: N-terminal ADF-H 1-142; C-terminal ADF-H 176-316
2hd7, 2d8b – mTwi-1 C-terminal ADF-H domain – mouse - NMR
1m4j – mTwi-1 N-terminal ADF-H domain
3daw – Twi-1 C-terminal ADF-H domain (mutant) + actin - rabbit
2vac – hTwi-2 N-terminal ADF-H domain - human
2w0i – hTwi-2 C-terminal ADF-H domain (mutant)
References
- ↑ Palmgren S, Vartiainen M, Lappalainen P. Twinfilin, a molecular mailman for actin monomers. J Cell Sci. 2002 Mar 1;115(Pt 5):881-6. PMID:11870207