2KHT

NMR Structure of human alpha defensin HNP-1


Experimental Data Snapshot

  • Method: SOLID-STATE NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR.

Zhang, Y.Doherty, T.Li, J.Lu, W.Barinka, C.Lubkowski, J.Hong, M.

(2010) J Mol Biol 397: 408-422

  • DOI: https://doi.org/10.1016/j.jmb.2010.01.030
  • Primary Citation of Related Structures:  
    2KHT

  • PubMed Abstract: 

    Human alpha-defensins [human neutrophil peptides (HNPs)] are immune defense mini-proteins that act by disrupting microbial cell membranes. Elucidating the three-dimensional (3D) structures of HNPs in lipid membranes is important for understanding their mechanisms of action. Using solid-state NMR (SSNMR), we have determined the 3D structure of HNP-1 in a microcrystalline state outside the lipid membrane, which provides benchmarks for structure determination and comparison with the membrane-bound state. From a suite of two-dimensional and 3D magic-angle spinning experiments, (13)C and (15)N chemical shifts that yielded torsion angle constraints were obtained, while inter-residue distances were obtained to restrain the 3D fold. Together, these constraints led to the first high-resolution SSNMR structure of a human defensin. The SSNMR structure has close similarity to the crystal structures of the HNP family, with the exception of the loop region between the first and second beta-strands. The difference, which is partially validated by direct torsion angle measurements of selected loop residues, suggests possible conformational variation and flexibility of this segment of the protein, which may regulate HNP interaction with the phospholipid membrane of microbial cells.


  • Organizational Affiliation

    Department of Chemistry, Iowa State University, Ames, IA 50011, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Neutrophil defensin 130Homo sapiensMutation(s): 0 
Gene Names: DEF1DEFA1DEFA2MRS
UniProt & NIH Common Fund Data Resources
Find proteins for P59665 (Homo sapiens)
Explore P59665 
Go to UniProtKB:  P59665
PHAROS:  P59665
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP59665
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLID-STATE NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-02-09
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2014-02-05
    Changes: Experimental preparation
  • Version 1.3: 2020-02-26
    Changes: Data collection, Database references, Other
  • Version 1.4: 2024-05-01
    Changes: Data collection, Database references