Alpha-defensins form biologically active dimers

Stable Identifier
R-HSA-1462014
Type
Reaction [transition]
Species
Homo sapiens
Compartment
extracellular region
ReviewStatus
5/5
Locations in the PathwayBrowser
Expand all
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
Alpha-defensins form biologically active dimers
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
The crystal structure of human alpha-defensin HNP-3 revealed that it forms a dimer containing a six-stranded beta-sheet region (Hill et al. 1991). NMR studies indicate that HNP-1 can also form dimers or higher-order aggregates in solution and artificial lipid bilayers (Zhang et al. 1992, 2010a, 2010b). Models of alpha and beta defensins suggest that dimerization and/or higher order structures are characteristic, though not univeral or required for the biological effects of some beta-defensins (Suresh & Verma 2006, Pazgier et al. 2006).
Literature References
PubMed ID Title Journal Year
17088326 Crystal structures of human alpha-defensins HNP4, HD5, and HD6

Lubkowski, J, Yang, D, Wu, Z, Tucker, K, Lu, W, Szyk, A

Protein Sci 2006
1445872 NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1

Zhang, XL, Selsted, ME, Pardi, A

Biochemistry 1992
2006422 Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization

Eisenberg, D, Yee, J, Selsted, ME, Hill, CP

Science 1991
Participants
Input
Output
Participates
as an event of
Orthologous Events
Alpha-defensins form biologically active dimers (Mus musculus)
Alpha-defensins form biologically active dimers (Rattus norvegicus)
Authored
Jupe, S  (2011-04-28)
Reviewed
McDermott, AM  (2011-11-03)
Created
Jupe, S  (2011-07-27)
Cite Us!