Recurrent substitutions of arginine 789 by cysteine in pro-alpha 1 (II) collagen chains produce spondyloepiphyseal dysplasia congenita.
D Chan, JF Rogers, JF Bateman… - The Journal of …, 1995 - europepmc.org
D Chan, JF Rogers, JF Bateman, WG Cole
The Journal of rheumatology. Supplement, 1995•europepmc.orgA child with typical spondyloepiphyseal dysplasia congenita had a recurrent, heterozygous
substitution of arginine 789 by cysteine in the triple helical domain of alpha 1 (II) chains of
type II collagen. The amino substitution was due to the transition of cytosine 2913 to thymine
in exon 41 of the COL2A1 gene. The amino acid substitution involved the Y position of a Gly-
XY triplet.
substitution of arginine 789 by cysteine in the triple helical domain of alpha 1 (II) chains of
type II collagen. The amino substitution was due to the transition of cytosine 2913 to thymine
in exon 41 of the COL2A1 gene. The amino acid substitution involved the Y position of a Gly-
XY triplet.
A child with typical spondyloepiphyseal dysplasia congenita had a recurrent, heterozygous substitution of arginine 789 by cysteine in the triple helical domain of alpha 1 (II) chains of type II collagen. The amino substitution was due to the transition of cytosine 2913 to thymine in exon 41 of the COL2A1 gene. The amino acid substitution involved the Y position of a Gly-XY triplet.
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