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-Structure paper
Title | Invariant gly residue is important for alpha-defensin folding, dimerization, and function: a case study of the human neutrophil alpha-defensin HNP1 |
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Journal, issue, pages | J. Biol. Chem., Vol. 287, Page 18900-18912, Year 2012 |
Publish date | Feb 21, 2012 (structure data deposition date) |
![]() | Zhao, L. / Ericksen, B. / Wu, X. / Zhan, C. / Yuan, W. / Li, X. / Pazgier, M. / Lu, W. |
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Methods | X-ray diffraction |
Resolution | 1.9 Å |
Structure data | ![]() PDB-4du0: |
Chemicals | ![]() ChemComp-GOL: ![]() ChemComp-CL: ![]() ChemComp-HOH: |
Source |
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![]() | ANTIBIOTIC / cysteine rich antimicrobial peptide / alpha-defensin / HNP1 / human alpha-defensin 1 / G17A mutant / defensin fold / antimicrobial peptide / human neutrophils |