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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Detalhes bibliográficos
Main Authors: Zhao, Le, Tolbert, W. David, Ericksen, Bryan, Zhan, Changyou, Wu, Xueji, Yuan, Weirong, Li, Xu, Pazgier, Marzena, Lu, Wuyuan
Formato: Artigo
Idioma:Inglês
Publicado em: Public Library of Science 2013
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Research Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3827289/
https://ncbi.nlm.nih.gov/pubmed/24236072
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0078937
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