Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22139156
PubMed Central
PMC3232129
DOI
10.1107/s1744309111046203
PII: S1744309111046203
Knihovny.cz E-resources
- MeSH
- Extracellular Space chemistry MeSH
- Crystallography, X-Ray MeSH
- Protein Structure, Quaternary MeSH
- NK Cell Lectin-Like Receptor Subfamily B chemistry genetics MeSH
- Models, Molecular MeSH
- Mutation * MeSH
- Mice MeSH
- Protein Structure, Tertiary MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- NK Cell Lectin-Like Receptor Subfamily B MeSH
The structure of the H107R variant of the extracellular domain of the mouse natural killer cell receptor NKR-P1A has been determined by X-ray diffraction at 2.3 Å resolution from a merohedrally twinned crystal. Unlike the structure of the wild-type receptor in space group I4(1)22 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I4(1) with a dimer in the asymmetric unit. Different degrees of merohedral twinning were detected in five data sets collected from different crystals. The mutation does not have a significant impact on the overall structure, but led to the binding of an additional phosphate ion at the interface of the molecules.
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Nkrp1 family, from lectins to protein interacting molecules
PDB
3T3A
