Characterisation of a glycine to valine substitution at amino acid position 910 of the triple helical region of type III collagen in a patient with Ehlers-Danlos syndrome type IV.
We have studied a patient with Ehlers-Danlos syndrome type IV. Protein mapping studies of her type III collagen had indicated that cyanogen bromide fragment 9 contained the site of the mutation. Here we describe the mapping of this region for a single base mutation using a chemical modification and cleavage technique. Sequence analysis of cDNA showed a G to T mutation resulting in the substitution of glycine 910 by valine. This was confirmed by allele specific oligonucleotide hybridisation to the proband's genomic DNA.
Richards
A J
AJ
Dermatology Research Group, Clinical Research Centre, Northwick Park Hospital, Harrow, Middlesex.
Lloyd
J C
JC
Ward
P N
PN
De Paepe
A
A
Narcisi
P
P
Pope
F M
FM
D000483:Alleles; D000595:Amino Acid Sequence; D001483:Base Sequence; D003094:Collagen / Q000235:genetics*; D004247:DNA / Q000235:genetics; D004252:DNA Mutational Analysis; D004535:Ehlers-Danlos Syndrome / Q000235:genetics*; D005260:Female; D005998:Glycine; D006801:Humans; D008875:Middle Aged; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D016133:Polymerase Chain Reaction; D014633:Valine
D003094:Collagen; D004247:DNA; D014633:Valine; D005998:Glycine