Twinfilin

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== Structural highlights ==
== Structural highlights ==
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The twinfilin-1 C-terminal ADF-H domain binds to a groove between two subdomains of actin. <scene name='80/805029/Cv/4'>Three major sites of interaction can be distinguished</scene>. These interactions include <scene name='80/805029/Cv/3'>hydrogen bonds</scene> (twinfilin residues are colored in magenta) and <scene name='80/805029/Cv/5'>hydrophobic contacts</scene> (actin residues are colored according to hydrophobic/polar)<ref>PMID:18625842</ref>.
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The twinfilin-1 C-terminal ADF-H domain binds to a groove between two subdomains of actin. <scene name='80/805029/Cv/4'>Three major sites of interaction can be distinguished</scene>. These interactions include <scene name='80/805029/Cv/3'>hydrogen bonds</scene> (twinfilin residues participating in interactions are colored in magenta) and <scene name='80/805029/Cv/5'>hydrophobic contacts</scene> (actin residues participating in interactions are colored according to hydrophobic/polar)<ref>PMID:18625842</ref>.
</StructureSection>
</StructureSection>

Revision as of 11:54, 2 January 2019

Structure of twinfilin-1 C-terminal ADF-H domain (green) complex with actin (cyan), ATP and Ca+2 ion (green (PDB code 3daw)

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3D structures of twinfilin

Updated on 02-January-2019

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 + ATP - rabbit
2vac – hTwi-2 N-terminal ADF-H domain - human
2w0i – hTwi-2 C-terminal ADF-H domain (mutant)


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
  2. ↑ Li L, Liu L, Qu B, Li X, Gao X, Zhang M. Twinfilin 1 enhances milk bio-synthesis and proliferation of bovine mammary epithelial cells via the mTOR signaling pathway. Biochem Biophys Res Commun. 2017 Oct 21;492(3):289-294. doi:, 10.1016/j.bbrc.2017.08.130. Epub 2017 Aug 31. PMID:28864421 doi:http://dx.doi.org/10.1016/j.bbrc.2017.08.130
  3. ↑ Paavilainen VO, Oksanen E, Goldman A, Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J Cell Biol. 2008 Jul 14;182(1):51-9. PMID:18625842 doi:10.1083/jcb.200803100

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Michal Harel, Alexander Berchansky

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