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.

Novel RNA-binding motif: The KH module

Adinolfi, S;
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.
1999
51
2
153
164
modular proteins; RNA-binding; fragile X; trinucleotide expansion
Adinolfi, S; Bagni, C; Morelli, MAC; Fraternali, F; Musco, G; Pastore, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/1905261
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