Single, Double and Quadruple Alanine Substitutions at Oligomeric Interfaces Identify Hydrophobicity as the Key Determinant of Human Neutrophil Alpha Defensin HNP1 Function

HNP1 is a human alpha defensin that forms dimers and multimers governed by hydrophobic residues, including Tyr(16), Ile(20), Leu(25), and Phe(28). Previously, alanine scanning mutagenesis identified each of these residues and other hydrophobic residues as important for function. Here we report furth...

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Detalles Bibliográficos
Autores principales: Zhao, Le, Tolbert, W. David, Ericksen, Bryan, Zhan, Changyou, Wu, Xueji, Yuan, Weirong, Li, Xu, Pazgier, Marzena, Lu, Wuyuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3827289/
https://www.ncbi.nlm.nih.gov/pubmed/24236072
http://dx.doi.org/10.1371/journal.pone.0078937

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3827289/
https://www.ncbi.nlm.nih.gov/pubmed/24236072
http://dx.doi.org/10.1371/journal.pone.0078937

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