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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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| Hoofdauteurs: | , , , , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
Public Library of Science
2013
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| Onderwerpen: | |
| Online toegang: | 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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