Ehlers-Danlos syndrome (EDS) is a heterogeneous group of connective tissue 
disorders. Recently mutations have been found in the genes for type V collagen 
in a small number of people with the most common forms of EDS, types I and II. 
Here we characterise a COL5A2 mutation in an EDS II family. Cultured dermal 
fibroblasts obtained from an affected subject synthesised abnormal type V 
collagen. Haplotype analysis excluded COL5A1 but was concordant with COL5A2 as 
the disease locus. The entire open reading frame of the COL5A2 cDNA was directly 
sequenced and a single base mutation detected. It substituted a glycine residue 
within the triple helical domain (G934R) of alpha2(V) collagen, typical of the 
dominant negative changes in other collagens, which cause various other 
inherited connective tissue disorders. All three affected family members 
possessed the single base change, which was absent in 50 normal chromosomes.