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

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.[1] 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.[2]

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.[1]

References

  1. 1 2 Maruyama K, Kurokawa H, Oosawa M, Shimaoka S, Yamamoto H, Ito M, Maruyama K (May 1990). "Beta-actinin is equivalent to Cap Z protein". J. Biol. Chem. 265 (15): 8712–5. doi:10.1016/S0021-9258(19)38947-1. PMID 2341404.
  2. Cooper JA, Caldwell JE, Gattermeir DJ, Torres MA, Amatruda JF, Casella JF (1991). "Variant cDNAs encoding proteins similar to the alpha subunit of chicken CapZ". Cell Motil. Cytoskeleton. 18 (3): 204–14. doi:10.1002/cm.970180306. PMID 1711931.
This article incorporates text from the public domain Pfam and InterPro: IPR018315
This article incorporates text from the public domain Pfam and InterPro: IPR001698
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