Back to Search
Start Over
Solution Structure of the R3H Domain from Human Sμbp-2
- Source :
- Journal of Molecular Biology. 326:217-223
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- The R3H domain is a conserved sequence motif, identified in over 100 proteins, that is thought to be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. In this work the 3D structure of the R3H domain from human Smubp-2 was determined by NMR spectroscopy. It is the first 3D structure determination of an R3H domain. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet and two alpha-helices, which is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. The similarities are non-trivial, as the amino acid identities are below 10%. Three conserved basic residues cluster on the same face of the R3H domain and could play a role in nucleic acid recognition. An extended hydrophobic area at a different site of the molecular surface could act as a protein-binding site. A strong correlation between conservation of hydrophobic amino acids and side-chain solvent protection indicates that the structure of the Smubp-2 R3H domain is representative of R3H domains in general.
- Subjects :
- Models, Molecular
EGF-like domain
Molecular Sequence Data
Protein domain
Prokaryotic Initiation Factor-3
Immunoglobulin domain
Structure-Activity Relationship
Bacterial Proteins
Structural Biology
EVH1 domain
Humans
Amino Acid Sequence
B3 domain
Nuclear Magnetic Resonance, Biomolecular
Molecular Biology
Chemistry
Escherichia coli Proteins
DHR1 domain
Protein Structure, Tertiary
DNA-Binding Proteins
Solutions
Crystallography
Cyclic nucleotide-binding domain
Sequence Alignment
Transcription Factors
Binding domain
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 326
- Database :
- OpenAIRE
- Journal :
- Journal of Molecular Biology
- Accession number :
- edsair.doi.dedup.....22928797fd583a785f2a4e605f133a19