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Invariant Gly Residue Is Important for α-Defensin Folding, Dimerization, and Function: A CASE STUDY OF THE HUMAN NEUTROPHIL α-DEFENSIN HNP1
The human α-defensins (HNP) are synthesized in vivo as inactive prodefensins, and contain a conserved glycine, Gly(17), which is part of a β-bulge structure. It had previously been shown that the glycine main chain torsion angles are in a d-configuration, and that d-amino acids but not l-alanine cou...
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| 主要な著者: | , , , , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Biochemistry and Molecular Biology
2012
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3365925/ https://ncbi.nlm.nih.gov/pubmed/22496447 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.355255 |
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