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TitleInvariant gly residue is important for alpha-defensin folding, dimerization, and function: a case study of the human neutrophil alpha-defensin HNP1
Journal, issue, pagesJ. Biol. Chem., Vol. 287, Page 18900-18912, Year 2012
Publish dateFeb 21, 2012 (structure data deposition date)
AuthorsZhao, L. / Ericksen, B. / Wu, X. / Zhan, C. / Yuan, W. / Li, X. / Pazgier, M. / Lu, W.
External linksJ. Biol. Chem. / PubMed:22496447
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-4du0:
Crystal structure of human alpha-defensin 1, HNP1 (G17A mutant)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsANTIBIOTIC / cysteine rich antimicrobial peptide / alpha-defensin / HNP1 / human alpha-defensin 1 / G17A mutant / defensin fold / antimicrobial peptide / human neutrophils

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