ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Complex assembly, crystallization and preliminary X-ray crystallographic studies of duck MHC class I molecule.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 6 citations in OpenAlex.
- Expression of Immune-Related Genes of Ducks Infected with Avian Pathogenic Escherichia coli (APEC).Frontiers in microbiology · 2016Article
- Complex assembly, crystallization and preliminary X-ray crystallographic analysis of the chicken CD8αα-BF2*0401 complex.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Expression, refolding and preliminary X-ray crystallographic analysis of equine MHC class I molecule complexed with an EIAV-Env CTL epitope.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Prediction and identification of T cell epitopes in the H5N1 influenza virus nucleoprotein in chicken.PloS one · 2012Article
- Expression, crystallization and preliminary crystallographic analysis of C-reactive protein from zebrafish.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Complex assembly, crystallization and preliminary X-ray crystallographic studies of the swine major histocompatibility complex molecule SLA-1*1502.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to understand the biological properties of the immune systems of waterfowl and to establish a system for structural studies of duck class I major histocompatibility complex (DuMHC I), a complex of DuMHC I with duck beta(2)-microglobulin (Dubeta(2)m) and the peptide AEIEDLIF (AF8) derived from H5N1 NP residues 251-258 was assembled. The complex was crystallized; the crystals belonged to space group C222(1), with unit-cell parameters a = 54.7, b = 72.4, c = 102.2 A, and diffracted to 2.3 A resolution. Matthews coefficient calculation and initial structure determination by molecular replacement showed that the crystals did not contain the whole DuMHC I complex, but instead contained the DuMHC I alpha3 domain and a Dubeta2m molecule (DuMHC I alpha3+beta2m). Another complex of DuMHC I with the peptide IDWFDGKE derived from a chicken fusion protein also generated the same results. The stable structure of DuMHC I alpha3+beta2m may reflect some unique characteristics of DuMHC I and pave the way for novel MHC structure-related studies in the future.
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