Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome (Q27732663)

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G Stier

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C Joseph

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M A Castiglione Morelli

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T J Gibson

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A Pastore

Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors

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language of work or name

English

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publication date

19 April 1996

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published in

Cell

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volume

85

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issue

2

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page(s)

237-45

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cites work

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The KH module has an αβ fold

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A point mutation in the FMR-1 gene associated with fragile X mental retardation

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The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation

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A target for Src in mitosis.

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The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid.

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Protein structure comparison by alignment of distance matrices

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Mutations in gld-1, a female germ cell-specific tumor suppressor gene in Caenorhabditis elegans, affect a conserved domain also found in Src-associated protein Sam68.

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Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains

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Intragenic loss of function mutations demonstrate the primary role of FMR1 in fragile X syndrome

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Localized Bicaudal-C RNA encodes a protein containing a KH domain, the RNA binding motif of FMR1.

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Molecular genetics of the fragile-X syndrome: a novel type of unstable mutation

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Absence of expression of the FMR-1 gene in fragile X syndrome

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The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein

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Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome

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