ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Expression, purification, crystallization and preliminary X-ray diffraction analysis of nurse shark β2-microglobulin.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- The Structure of a Peptide-Loaded Shark MHC Class I Molecule Reveals Features of the Binding between βJournal of immunology (Baltimore, Md. : 1950) · 2021Article
- A Comparison of the Innate and Adaptive Immune Systems in Cartilaginous Fish, Ray-Finned Fish, and Lobe-Finned Fish.Frontiers in immunology · 2019Review
- Crystallization and preliminary X-ray diffraction analysis of the two distinct types of zebrafish β2-microglobulin.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Crystallization and preliminary X-ray diffraction analysis of a single variable domain of the immunoglobulin superfamily in amphioxus, Amphi-IgSF-V.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Crystals on the cover 2013.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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Authors and funding
7 authors.
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Abstract
β(2)-Microglobulin (β(2)m) is an essential subunit of the major histocompatibility complex (MHC) class I molecule that helps to stabilize the structure of peptide-MHC I (pMHC I). It is also one of the typical immunoglobulin superfamily (IgSF) molecules in the adaptive immune system (AIS). Sharks belong to the cartilaginous fish, which are the oldest jawed vertebrate ancestors with an AIS to exist in the world. Thus, the study of cartilaginous fish β(2)m would help in understanding the evolution of IgSF molecules. In order to demonstrate this, β(2)m from a cartilaginous fish, nurse shark (Ginglymostoma cirratum), was expressed, refolded, purified and crystallized. Diffraction data were collected to a resolution of 2.3 Å. The crystal belonged to space group P3(2)21, with unit-cell parameters a = b = 88.230, c = 67.146 Å. The crystal structure contained two molecules in the asymmetric unit. The results will provide structural information for study of the evolution of β(2)m and IgSF in the AIS.
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