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Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution
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SYSNO ASEP 0369318 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution Author(s) Kolenko, Petr (UMCH-V) RID
Rozbeský, Daniel (MBU-M)
Vaněk, Ondřej (MBU-M)
Bezouška, Karel (MBU-M)
Hašek, Jindřich (UMCH-V) RID
Dohnálek, Jan (FZU-D) RIDSource Title Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091
Roč. 67, č. 12 (2011), s. 1519-1523Number of pages 5 s. Language eng - English Country GB - United Kingdom Keywords NKR-P1A ; merohedral twinning ; mutation Subject RIV EB - Genetics ; Molecular Biology R&D Projects GA305/07/1073 GA ČR - Czech Science Foundation (CSF) GAP302/11/0855 GA ČR - Czech Science Foundation (CSF) 1M0505 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40500505 - UMCH-V (2005-2011) AV0Z50200510 - MBU-M (2005-2011) AV0Z10100521 - FZU-D (2005-2011) UT WOS 000297741100011 DOI 10.1107/S1744309111046203 Annotation 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 A° resolution from a merohedrally twinned crystal. Unlike the structure of the wild-type receptor in space group I4122 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I41 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. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2012
Number of the records: 1