A point mutation of the Noggin2 protein increasing its binding capacity to activin

Autor:	Natalia Y. Martynova, Andrey V. Bayramov, Andrey G. Zaraisky, Fedor M. Eroshkin, N. V. Fedina
Rok vydání:	2015
Předmět:	animal structures Point mutation Organic Chemistry Mutant Xenopus Mutagenesis (molecular biology technique) Plasma protein binding Biology biology.organism_classification Biochemistry Molecular biology GDF6 embryonic structures Noggin Activin type 2 receptors
Zdroj:	Russian Journal of Bioorganic Chemistry. 41:675-677
ISSN:	1608-330X 1068-1620
DOI:	10.1134/s1068162015060059
Popis:	Earlier we have revealed the ability of Noggin family proteins to bind a member of the TUF-β superfamily, ActivinB, and to repress the Activin-dependent Smad2 signaling cascade. In the present work we have characterized a mutant of the Xenopus laevis Noggin2, bearing the substitution W203R. We have shown that this point mutation enhances the affinity of Noggin2 to ActivinB, while weakens its affinity to BMP. Consistently, we have shown that W203 R mutant inhibits Smad2 signaling cascade more efficiently than the wild-type Noggin2. Interestingly, the mutation of human Noggin in the homologous position is associated with hereditary anomalies. The revealed effects of W203R substitution in Noggin2 demonstrate promising potential of such mutagenesis for generation of Noggin variants with enhanced affinity to different members of the TGF-β superfamily.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::01b2a522a4d9f77c5083926d3af1f118 https://doi.org/10.1134/s1068162015060059 Zobrazit plný text záznamu Full text from SpringerLink