Novel RNA-binding motif: the KH module

Détails

ID Serval
serval:BIB_C1C595E55D3E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Novel RNA-binding motif: the KH module
Périodique
Biopolymers
Auteur(s)
Adinolfi S., Bagni C., Castiglione Morelli M. A., Fraternali F., Musco G., Pastore A.
ISSN
0006-3525 (Print)
ISSN-L
0006-3525
Statut éditorial
Publié
Date de publication
1999
Volume
51
Numéro
2
Pages
153-64
Notes
Adinolfi, S
Bagni, C
Castiglione Morelli, M A
Fraternali, F
Musco, G
Pastore, A
eng
MC_U117584256/Medical Research Council/United Kingdom
1999/07/09
Biopolymers. 1999;51(2):153-64.
Résumé
The KH motif has recently been identified in single or multiple copies in a number of RNA associated proteins. Here we review the current knowledge accumulated about the sequence, structure, and functions of the KH. The multidomain architecture of most of the KH-containing proteins inspired an approach based on the production of peptides spanning the sequence of an isolated KH motif. Correct identification of the minimal length necessary for producing a folded peptide has had a number of important consequences for interpreting functional data. The presence of the KH motifs in fmr1, the protein responsible for the fragile X syndrome, and their possible role in the fmr1 functions are also discussed.
Mots-clé
Amino Acid Sequence, *Carrier Proteins, Female, Fragile X Mental Retardation Protein, Fragile X Syndrome/epidemiology/genetics, Humans, Male, Models, Molecular, Molecular Sequence Data, Mutation, Nerve Tissue Proteins/chemistry, Protein Structure, Secondary, RNA-Binding Proteins/*chemistry, Ribonucleoproteins, Small Nuclear/chemistry, Sequence Alignment
Pubmed
Création de la notice
06/03/2017 18:23
Dernière modification de la notice
03/03/2018 21:08
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