Twinfilin

From Proteopedia

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Revision as of 09:37, 31 December 2018

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights 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

3D structures of twifilin

2hd7, 2d8b – mTwi-1 C-terminal ADF-H domain 176-316 – mouse - NMR
1m4j – mTwi-1 N-terminal ADF-H domain 1-142
3daw – Twi-1 C-terminal ADF-H domain (mutant) + actin - rabbit
2vac – hTwi-2 N-terminal ADF-H domain 1-142 - human
2w0i – hTwi-2 C-terminal ADF-H domain (mutant)
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Updated on 31-December-2018

References

1. ↑ 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