Premium
The KH module has an αβ fold
Author(s) -
Castiglione Morelli Maria Antonietta,
Stier Gunter,
Gibson Toby,
Joseph Catherine,
Musco Giovanna,
Pastore Annalisa,
Travè Gilles
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01422-w
Subject(s) - antiparallel (mathematics) , protein secondary structure , chemical shift , amide , crystallography , beta sheet , nuclear magnetic resonance spectroscopy , chemistry , two dimensional nuclear magnetic resonance spectroscopy , helix (gastropod) , protein structure , stereochemistry , biology , biochemistry , physics , ecology , quantum mechanics , snail , magnetic field
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 1 H and 15 N resonances using uniform 15 N‐labeling of the protein combined with homo‐nuclear 2D 1 HNMR and 3D 15 N correlated 1 H NMR. On the basis of NOE patterns, secondary chemical shifts and amide solvent exposure, the secondary structure consists of an antiparallel three stranded β 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.