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Proteins. 2016 Sep;84(9):1304-11. doi: 10.1002/prot.25078. Epub 2016 Jun 15.

Solution structure of the lymphocyte receptor Nkrp1a reveals a distinct conformation of the long loop region as compared to in the crystal structure.

Author information

1
Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
2
Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic.
3
Department of Cell Biology, Faculty of Science, Charles University, Prague, Czech Republic.

Abstract

Mouse Nkrp1a receptor is a C-type lectin-like receptor expressed on the surface of natural killer cells that play an important role against virally infected and tumor cells. The recently solved crystal structure of Nkrp1a raises questions about a long loop region which was uniquely extended from the central region in the crystal. To understand the functional significance of the loop, the solution structure of Nkrp1a using nuclear magnetic resonance (NMR) spectroscopy was determined. A notable difference between the crystal and NMR structure of Nkrp1a appears in the conformation of the long loop region. While the extended loop points away from the central core and mediates formation of a domain swapped dimer in the crystal, the solution structure is monomeric with the loop tightly anchored to the central region. The findings described the first solution structure in the Nkrp1 family and revealed intriguing similarities and differences to the crystal structure. Proteins 2016; 84:1304-1311.

KEYWORDS:

CTLD; NK receptor; Nkrp1; Nkrp1a; domain-swapping; long loop region; nuclear magnetic resonance

PMID:
27238500
DOI:
10.1002/prot.25078
[Indexed for MEDLINE]

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