Alpha-defensins form biologically active dimers

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R-HSA-1462014
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Reaction [transition]
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Homo sapiens
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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
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
17088326 Crystal structures of human alpha-defensins HNP4, HD5, and HD6

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

Protein Sci 2006
2006422 Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization

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

Science 1991
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