The KH module has an alpha beta fold.
The KH module has recently been identified in a number of RNA associated proteins including vigilin and FMR1, a protein implicated in the fragile X syndrome. In this work, NMR spectroscopy was used to determine the secondary structure in solution of a KH domain (repeat 5 from vigilin). Almost complete assignments were obtained for the 1H and 15N resonances using uniform 15N-labeling of the protein combined with homo-nuclear 2D 1HNMR and 3D 15N correlated 1H NMR. On the basis of NOE patterns, secondary chemical shifts and amide solvent exposure, the secondary structure consists of an antiparallel three stranded beta sheet connected by two helical regions. This domain may also be stabilized by an appended C-terminal helix which is common to many but not all members of the KH family.
Castiglone Morelli
M A
MA
EMBL, Heidelberg, Germany.
Stier
G
G
Gibson
T
T
Joseph
C
C
Musco
G
G
Pastore
A
A
Travè
G
G
D000595:Amino Acid Sequence; D002352:Carrier Proteins; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D016601:RNA-Binding Proteins
D002352:Carrier Proteins; D011506:Proteins; D016601:RNA-Binding Proteins; C075197:high density lipoprotein binding protein