The substitution of glycine 661 by arginine in type III collagen produces mutant molecules with different thermal stabilities and causes Ehlers-Danlos syndrome type IV
| Autor: | C Ferguson, Allan J. Richards, F M Pope, P. Narcisi, J. C. Lloyd |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Hot Temperature
Arginine Mutant Molecular Sequence Data Glycine Peptide Biology chemistry.chemical_compound Mutant protein Genetics medicine Humans Point Mutation Genetics (clinical) chemistry.chemical_classification Base Sequence Point mutation medicine.disease Biochemistry chemistry Ehlers–Danlos syndrome Cyanogen bromide Ehlers-Danlos Syndrome Female Collagen Research Article |
| Zdroj: | Journal of medical genetics. 30(8) |
| ISSN: | 0022-2593 |
| Popis: | Previous studies have shown that Ehlers-Danlos syndrome type IV (EDS IV) is caused by mutations of type III collagen (COL3A1). Here we have characterised the most amino-terminal glycine substitution so far described in a patient with EDS IV. A combination of peptide mapping and chemical cleavage analysis of cDNA localised the mutation in cyanogen bromide peptide CB5. Sequence analysis showed a G to A mutation, converting glycine 661 to arginine, which was a new dominant mutation. Analysis of type III collagen secreted by cultured fibroblasts showed an overmodified mutant protein with normal thermal stability. However, the intracellularly retained form melted 2 degrees C lower than normal. This indicated that molecules resulting from the same mutation can differ in their thermal stabilities. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|