F-actin capping protein

In molecular biology, the F-actin capping protein is a protein complex which binds in a calcium-independent manner to the fast-growing ends of actin filaments (barbed end), thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta. Neither of the subunits shows sequence similarity to other filament-capping proteins. The alpha subunit is a protein of about 268 to 286 amino acid residues and the beta subunit is approximately 280 amino acids, their sequences are well conserved in eukaryotic species.

F-actin capping protein alpha subunit
solution nmr structure of s100b bound to the high-affinity target peptide trtk-12
Identifiers
SymbolF-actin_cap_A
PfamPF01267
InterProIPR018315
PROSITEPDOC00609
SCOP21izn / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
F-actin capping protein, beta subunit
Identifiers
SymbolF_actin_cap_B
PfamPF01115
InterProIPR001698
PROSITEPDOC00203
SCOP21izn / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis, as well as muscle contraction.

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