1MSZ

Solution structure of the R3H domain from human Smubp-2

Summary for 1MSZ

• Entry DOI: 10.2210/pdb1msz/pdb
• NMR Information: BMRB: 5535
• Descriptor: DNA-binding protein SMUBP-2 (1 entity in total)
• Functional Keywords: r3h fold, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P38935
• Total number of polymer chains: 1
• Total formula weight: 9706.85

Authors

Liepinsh, E.,Leonchiks, A.,Sharipo, A.,Guignard, L.,Otting, G. (deposition date: 2002-09-20, release date: 2002-10-09, Last modification date: 2024-05-29)

Primary citation

Liepinsh, E.,Leonchiks, A.,Sharipo, A.,Guignard, L.,Otting, G.
Solution structure of the R3H domain from human Smubp-2
J.Mol.Biol., 326:217-223, 2003

PubMed 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.

PubMed: 12547203
DOI: 10.1016/S0022-2836(02)01381-5

Experimental method

SOLUTION NMR