Twinfilin
From Proteopedia
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<StructureSection load='3daw' size='400' side='right' caption='Structure of twinfilin-1 C-terminal ADF-H domain (green) complex with actin (cyan), ATP and Ca+2 ion (green (PDB code [[3daw]])' scene='80/805029/Cv/1'> | <StructureSection load='3daw' size='400' side='right' caption='Structure of twinfilin-1 C-terminal ADF-H domain (green) complex with actin (cyan), ATP and Ca+2 ion (green (PDB code [[3daw]])' scene='80/805029/Cv/1'> | ||
| - | + | __TOC__ | |
== Function == | == 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<ref>PMID:11870207</ref>. | '''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<ref>PMID:11870207</ref>. | ||
| + | *'''Twinfilin 1''' is an actin-depolymerisation factor regulating actin filament assembly <ref>PMID:35168059</ref>. | ||
| + | *'''Twinfilin 2''' regulates stereocilia elongation for maintaining the architecture of cochlear hair bundles<ref>PMID:19955359</ref>. | ||
== Relevance == | == Relevance == | ||
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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/6'>Three major sites of interaction can be distinguished</scene>. These interactions include <scene name='80/805029/Cv/7'>hydrogen bonds</scene> (twinfilin residues participating in interactions are colored in magenta) and <scene name='80/805029/Cv/8'>hydrophobic contacts</scene> (actin residues participating in interactions are colored according to hydrophobic/polar)<ref>PMID:18625842</ref>. | The twinfilin-1 C-terminal ADF-H domain binds to a groove between two subdomains of actin. <scene name='80/805029/Cv/6'>Three major sites of interaction can be distinguished</scene>. These interactions include <scene name='80/805029/Cv/7'>hydrogen bonds</scene> (twinfilin residues participating in interactions are colored in magenta) and <scene name='80/805029/Cv/8'>hydrophobic contacts</scene> (actin residues participating in interactions are colored according to hydrophobic/polar)<ref>PMID:18625842</ref>. | ||
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| - | </StructureSection> | ||
==3D structures of twinfilin== | ==3D structures of twinfilin== | ||
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[[2vac]] – hTwi-2 N-terminal ADF-H domain - human<br /> | [[2vac]] – hTwi-2 N-terminal ADF-H domain - human<br /> | ||
[[2w0i]] – hTwi-2 C-terminal ADF-H domain (mutant) <br /> | [[2w0i]] – hTwi-2 C-terminal ADF-H domain (mutant) <br /> | ||
| + | [[7ccc]] – hTwi-1 + F-actin-capping protein + actin<br /> | ||
[[2hd7]], [[2d8b]] – mTwi-1 C-terminal ADF-H domain – mouse - NMR<br /> | [[2hd7]], [[2d8b]] – mTwi-1 C-terminal ADF-H domain – mouse - NMR<br /> | ||
[[1m4j]] – mTwi-1 N-terminal ADF-H domain <br /> | [[1m4j]] – mTwi-1 N-terminal ADF-H domain <br /> | ||
[[6rsw]] – mTwi-1 C-terminal ADF-H domain + actin + CAP1<br /> | [[6rsw]] – mTwi-1 C-terminal ADF-H domain + actin + CAP1<br /> | ||
| - | [[3daw]] – | + | [[7ds2]] – mTwi-1 C-terminal + F-actin-capping protein<br /> |
| + | [[7ds4]] – mTwi-1 C-terminal (mutant) + F-actin-capping protein<br /> | ||
| + | [[7dsb]] – mTwi-1 C-terminal + F-actin-capping protein + myotrophin<br /> | ||
| + | [[7ds3]] – mTwi-2 + F-actin-capping protein<br /> | ||
| + | [[6yp9]] – rTwi-1 C-terminal ADF-H domain + actin - rabbit<br /> | ||
| + | [[3daw]] – rTwi-1 C-terminal ADF-H domain (mutant) + actin + ATP<br /> | ||
| + | [[6k2f]] – Twi – ''Entamoeba histolytica''<br /> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| - | + | </StructureSection> | |
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
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