2mti

Publication Abstract from PubMed

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, we determined the solution structure of Nkrp1a using NMR spectroscopy. 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. Our findings describe the first solution structure in the Nkrp1 family and reveal intriguing similarities and differences to the crystal structure. This article is protected by copyright. All rights reserved.

Solution structure of the lymphocyte receptor Nkrp1a reveals a distinct conformation of the long loop region as compared to in the crystal structure.,Rozbesky D, Adamek D, Pospisilova E, Novak P, Chmelik J Proteins. 2016 May 30. doi: 10.1002/prot.25078. PMID:27238500^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.