F-actin capping protein

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Current revision (08:12, 5 June 2025) (edit) (undo)
 
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[[F-actin capping protein 3D structures]]
[[F-actin capping protein 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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[[6f3a]], [[6f38]], [[6f1u]], [[6f1t]], [[5nw4]], [[5afu]] - pCAPZ β in dynactin dynein complex – pig – Cryo EM<br />
 
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[[6znl]] - pCAPZ α1+β2 in dynactin complex – Cryo EM<br />
 
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[[5adx]] - pCAPZ α1+β2 + dynactin + actin – Cryo EM<br />
 
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[[1izn]] – cCapZ α1+β – chicken<br />
 
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[[3aa7]] - cCapZ α1+β (mutant)<br />
 
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[[2kbm]] - CapZ α2 + S-100 calcium-binding protein - rat<br />
 
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[[3lk2]], [[3lk3]] - cCapZ α1+β + leucine-rich repeat-containing protein 16A<br />
 
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[[3aa0]] - cCapZ α1+β (mutant) + leucine-rich repeat-containing protein 16A peptide<br />
 
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[[3aae]] - cCapZ α1+β + leucine-rich repeat-containing protein 16A peptide<br />
 
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[[3aa1]] - cCapZ α1+β (mutant) + CKIP-1 peptide<br />
 
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[[2kz7]] - cCapZ α1+β + leucine-rich repeat-containing protein 16A]] - NMR<BR />
 
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[[3lk4]] - cCapZ α1+β + CD2-associated protein<br />
 
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[[3aa6]] - cCapZ α1+β (mutant) + CD2-associated protein peptide<br />
 
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[[2kxp]] - cCapZ α1+β + myotrophin – NMR<BR />
 
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[[3aaa]], [[7dsa]] - cCapZ α1+β + myotrophin<br />
 
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[[7ds2]], [[7ds4]], [[7ds6]], [[7ds8]] - cCAPZ α1+β + twinfilin-1<br />
 
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[[7ds3]] - cCAPZ α1+β + twinfilin-2<br />
 
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[[7ccc]] - cCAPZ α1+β + twinfilin-1 + ADP<br />
 
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[[7dsb]] - cCAPZ α1+β + twinfilin-1 + myotrophin<br />
 
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[[4akr]] - CAPZ α1+β – slime mold<br />
 
== References ==
== References ==

Current revision

F-actin capping protein α (cyan) and β subunits (magenta) complex with ethanosulfonic acid and Ba+2 ion (PDB code 3aa7)

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3D structures of F-actin capping protein

F-actin capping protein 3D structures

References

  1. Takeda S, Minakata S, Koike R, Kawahata I, Narita A, Kitazawa M, Ota M, Yamakuni T, Maeda Y, Nitanai Y. Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition. PLoS Biol. 2010 Jul 6;8(7):e1000416. PMID:20625546 doi:10.1371/journal.pbio.1000416

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Michal Harel, Alexander Berchansky

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