Solution structure of the R3H domain from human Smubp-2.

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.

Edvards Liepinsh, Ainars Leonchiks, Anatoly Sharipo, Laurent Guignard and
Gottfried Otting.
Solution structure of the R3H domain from human Subp-2
J. Biol. Chem., submitted.

Solution Structure Of The R3h Domain From Human Smubp-2 In Complex With 2'-Deoxyguanosine-5'-Monophosphate

immunoglobulin mu binding protein 2 variant [Homo sapiens]

DNA-binding protein SMUBP-2 [Homo sapiens]

PREDICTED: DNA-binding protein SMUBP-2, partial [Pongo abelii]

PREDICTED: DNA-binding protein SMUBP-2 [Nomascus leucogenys]

PREDICTED: DNA-binding protein SMUBP-2 [Pan paniscus]

PREDICTED: DNA-binding protein SMUBP-2 [Gorilla gorilla gorilla]

RecName: Full=DNA-binding protein SMUBP-2; AltName: Full=ATP-dependent helicase IGHMBP2; AltName: Full=Glial factor 1; Short=GF