Novel RNA-binding motif: the KH module.
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.
Adinolfi
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The National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, U.K.
Bagni
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Castiglione Morelli
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Fraternali
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Musco
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Pastore
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D000595:Amino Acid Sequence; D002352:Carrier Proteins; D005260:Female; D051860:Fragile X Messenger Ribonucleoprotein 1; D005600:Fragile X Syndrome / Q000453:epidemiology / Q000235:genetics; D006801:Humans; D008297:Male; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000737:chemistry; D017433:Protein Structure, Secondary; D016601:RNA-Binding Proteins / Q000737:chemistry*; D017411:Ribonucleoproteins, Small Nuclear / Q000737:chemistry; D016415:Sequence Alignment
D002352:Carrier Proteins; D051860:Fragile X Messenger Ribonucleoprotein 1; D009419:Nerve Tissue Proteins; D016601:RNA-Binding Proteins; D017411:Ribonucleoproteins, Small Nuclear; C497683:FMR1 protein, human; C075197:high density lipoprotein binding protein