Signal recognition particle (SRP) receptor alpha subunit, N-terminal
Structure of the beta subunit of the eukaryotic signal recognition particle receptor.[1]
Identifiers
Symbol
SRX
Pfam
PF09201
InterPro
IPR015284
SCOP2
1nrj / SCOPe / SUPFAM
OPM superfamily
136
OPM protein
1nrj
Membranome
38
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Signal recognition particle (SRP) receptor, also called the docking protein, is a dimer composed of 2 different subunits that are associated exclusively with the rough ER in mammalian cells. Its main function is to identify the SRP units. SRP (signal recognition particle) is a molecule that helps the ribosome-mRNA-polypeptide complexes to settle down on the membrane of the endoplasmic reticulum.
The eukaryotic SRP receptor (termed SR) is a heterodimer of SR-alpha (70 kDa; SRPRA) and SR-beta (25 kDa; SRPRB), both of which contain a GTP-binding domain,[2] while the prokaryotic SRP receptor comprises only the monomeric loosely membrane-associated SR-alpha homologue FtsY (P10121).
^Schwartz T, Blobel G (March 2003). "Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor". Cell. 112 (6): 793–803. doi:10.1016/S0092-8674(03)00161-2. PMID 12654246.
^Blobel G, Schwartz T (2003). "Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor". Cell. 112 (6): 793–803. doi:10.1016/S0092-8674(03)00161-2. PMID 12654246.
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