In molecular biology, S4 domain refers to a small RNA-binding protein domain found in a ribosomal protein named uS4 (called S9 in eukaryotes). The S4 domain is approximately 60-65 amino acid residues long, occurs in a single copy at various positions in different proteins and was originally found in pseudouridine syntheses, a bacterial ribosome-associated protein.[1]
The S4 protein helps to initiate assembly of the 16S rRNA. In this way proteins serve to organise and stabilise the rRNA tertiary structure.[2][3]
^Aravind L, Koonin EV (March 1999). "Novel predicted RNA-binding domains associated with the translation machinery". J. Mol. Evol. 48 (3): 291–302. doi:10.1007/pl00006472. PMID 10093218. S2CID 8083860.
^Maguire BA, Zimmermann RA (March 2001). "The ribosome in focus". Cell. 104 (6): 813–6. doi:10.1016/s0092-8674(01)00278-1. PMID 11290319. S2CID 8174178.
^Chandra Sanyal S, Liljas A (December 2000). "The end of the beginning: structural studies of ribosomal proteins". Curr. Opin. Struct. Biol. 10 (6): 633–6. doi:10.1016/S0959-440X(00)00143-3. PMID 11114498.
biology, S4domain refers to a small RNA-binding proteindomain found in a ribosomal protein named uS4 (called S9 in eukaryotes). The S4domain is approximately...
The S4 ribosomal protein leader is a ribosomal protein leader involved in ribosome biogenesis. It is used as an autoregulatory mechanism to control the...
least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. ProteinsS4 and S7, which initiate assembly of the...
uL14 (MRPL14). Organelle-specific proteins use their own cross-domain prefixes, for example "mS33" for MRPS33: Table S3,S4 and "cL37" for PSRP5.: Table S2...
ferredoxin superfamily (contains two Fe4-S4 clusters). Protein families are more closely related than superfamilies. Domains are placed in the same family if...
outer membrane protein W (OmpW) proteins from a variety of bacterial species. This protein may form the receptor for S4 colicins in Escherichia coli. Braun...
a common domain architecture. The factor IX protein is composed of four proteindomains: the Gla domain, two tandem copies of the EGF domain and a C-terminal...
In a chain-like biological molecule, such as a protein or nucleic acid, a structural motif is a common three-dimensional structure that appears in a variety...
up of two proteindomains: a voltage sensor domain, and a phosphatase domain coupled to a lipid-binding C2 domain. The voltage sensor domain contains four...
of the ball interacts with the alanine in domain III's S4-S5 segments and the asparagine in domain IV's S4-S5 segments. This explains why inactivation...
in that there are only two AT domains, and both are found on the same protein, MmpC. These AT domains are the only domains present on MmpC, while the other...
kinases. They were also able to identify 131 proteins with three or more predicted transmembrane domains. Vaisar et al. uses shotgun proteomics to implicate...
After transient loading of the cells with the non-toxic dermaseptin S4 analogue K4–S4(1–13)a, the peptide is transported in the systemic circulation to...
cytotoxic effects. The amino-terminal domain of the protein takes part in receptor binding as the carboxy-terminal domain is responsible for cytotoxic effect...
profiles, proteindomain structures, text mining of publications, phylogenetic profiles, phenotypic profiles, and protein-protein interaction. Protein function...
have been deposited in the protein data bank. The active site of factor Xa is divided into four subpockets as S1, S2, S3 and S4. The S1 subpocket determines...
Cystic fibrosis transmembrane conductance regulator (CFTR) is a membrane protein and anion channel in vertebrates that is encoded by the CFTR gene. Geneticist...
residues to allow for this. KCNE1 destabilizes the S4-S5 alpha-helix linkage in the KCNQ1 channel protein in addition to destabilizing the S6 alpha helix...
predicting protein structure. Molecular design and docking. The way that features, often vectors in a many-dimensional space, are extracted from the domain data...
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