1VIH

NMR STUDY OF VIGILIN, REPEAT 6, MINIMIZED AVERAGE STRUCTURE

Summary for 1VIH

• Entry DOI: 10.2210/pdb1vih/pdb
• Descriptor: VIGILIN (1 entity in total)
• Functional Keywords: rna-binding protein, ribonucleoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q00341
• Total number of polymer chains: 1
• Total formula weight: 8208.35

Authors

Musco, G.,Stier, G.,Joseph, C.,Morelli, M.A.C.,Nilges, M.,Gibson, T.J.,Pastore, A. (deposition date: 1995-11-29, release date: 1996-04-03, Last modification date: 2024-05-22)

Primary citation

Musco, G.,Stier, G.,Joseph, C.,Castiglione Morelli, M.A.,Nilges, M.,Gibson, T.J.,Pastore, A.
Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome.
Cell(Cambridge,Mass.), 85:237-245, 1996

PubMed Abstract: The KH module is a sequence motif found in a number of proteins that are known to be in close association with RNA. Experimental evidence suggests a direct involvement of KH in RNA binding. The human FMR1 protein, which has two KH domains, is associated with fragile X syndrome, the most common inherited cause of mental retardation. Here we present the three-dimensional solution structure of the KH module. The domain consists of a stable beta alpha alpha beta beta alpha fold. On the basis of our results, we suggest a potential surface for RNA binding centered on the loop between the first two helices. Substitution of a well-conserved hydrophobic residue located on the second helix destroys the KH fold; a mutation of this position in FMR1 leads to an aggravated fragile X phenotype.

PubMed: 8612276
DOI: 10.1016/S0092-8674(00)81100-9

Experimental method

SOLUTION NMR