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.File | Dimensione | Formato | |
---|---|---|---|
Adinolfi_Novel RNA‐binding motif.pdf
Accesso riservato
Tipo di file:
PDF EDITORIALE
Dimensione
516.81 kB
Formato
Adobe PDF
|
516.81 kB | Adobe PDF | Visualizza/Apri Richiedi una copia |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.