3T3A
Crystal structure of H107R mutant of extracellular domain of mouse receptor NKR-P1A
Summary for 3T3A
| Entry DOI | 10.2210/pdb3t3a/pdb |
| Related | 3M9Z |
| Descriptor | Killer cell lectin-like receptor subfamily B member 1A, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | c-type lectin-like domain, domain swapping, twinning, natural killer cell receptor, transmembrane receptor, signaling protein |
| Biological source | Mus musculus (mouse) |
| Cellular location | Membrane; Single-pass type II membrane protein: P27811 |
| Total number of polymer chains | 2 |
| Total formula weight | 32340.55 |
| Authors | Kolenko, P.,Rozbesky, D.,Bezouska, K.,Hasek, J.,Dohnalek, J. (deposition date: 2011-07-25, release date: 2011-08-10, Last modification date: 2024-11-06) |
| Primary citation | Kolenko, P.,Rozbesky, D.,Vanek, O.,Bezouska, K.,Hasek, J.,Dohnalek, J. Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 A resolution. Acta Crystallogr.,Sect.F, 67:1519-1523, 2011 Cited by PubMed Abstract: 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. PubMed: 22139156DOI: 10.1107/S1744309111046203 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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