The KH motif has recently been identified in single ol multiple copies in a number of RNA associated proteins. Here Mle 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 lend 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. (C) 1999 John Wiley & Sons, Inc.
Adinolfi, S., Bagni, C., Morelli, M., Fraternali, F., Musco, G., Pastore, A. (1999). Novel RNA-binding motif: The KH module. BIOPOLYMERS, 51(2), 153-164 [10.1002/(SICI)1097-0282(1999)51:2<153::AID-BIP5>3.0.CO;2-6].
Novel RNA-binding motif: The KH module
BAGNI, CLAUDIA;
1999-01-01
Abstract
The KH motif has recently been identified in single ol multiple copies in a number of RNA associated proteins. Here Mle 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 lend 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. (C) 1999 John Wiley & Sons, Inc.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
