2MTI
NMR structure of the lymphocyte receptor NKR-P1A
Summary for 2MTI
Entry DOI | 10.2210/pdb2mti/pdb |
NMR Information | BMRB: 19282 |
Descriptor | Killer cell lectin-like receptor subfamily B member 1A (1 entity in total) |
Functional Keywords | c-type lectin-like domain, nk cells, nk receptor, nkr-p1a, immune system |
Biological source | Mus musculus (mouse) |
Total number of polymer chains | 1 |
Total formula weight | 16008.77 |
Authors | Chmelik, J.,Rozbesky, D.,Pospisilova, E.,Adamek, D.,Novak, P. (deposition date: 2014-08-19, release date: 2015-11-11, Last modification date: 2024-10-16) |
Primary citation | Rozbesky, D.,Adamek, D.,Pospisilova, E.,Novak, P.,Chmelik, J. Solution structure of the lymphocyte receptor Nkrp1a reveals a distinct conformation of the long loop region as compared to in the crystal structure. Proteins, 84:1304-1311, 2016 Cited by PubMed 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. © 2016 Wiley Periodicals, Inc. PubMed: 27238500DOI: 10.1002/prot.25078 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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