| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-91 |
Sentence |
denotes |
Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2. |
| T2 |
92-221 |
Sentence |
denotes |
Killer cell inhibitory receptors (KIR) protect class I HLAs expressing target cells from natural killer (NK) cell-mediated lysis. |
| T3 |
222-454 |
Sentence |
denotes |
To understand the molecular basis of this receptor-ligand recognition, we have crystallized the extracellular ligand-binding domains of KIR2DL2, a member of the Ig superfamily receptors that recognize HLA-Cw1, 3, 7, and 8 allotypes. |
| T4 |
455-620 |
Sentence |
denotes |
The structure was determined in two different crystal forms, an orthorhombic P212121 and a trigonal P3221 space group, to resolutions of 3.0 and 2.9 A, respectively. |
| T5 |
621-857 |
Sentence |
denotes |
The overall fold of this structure, like KIR2DL1, exhibits K-type Ig topology with cis-proline residues in both domains that define beta-strand switching, which sets KIR apart from the C2-type hematopoietic growth hormone receptor fold. |
| T6 |
858-1040 |
Sentence |
denotes |
The hinge angle of KIR2DL2 is approximately 80 degrees, 14 degrees larger than that observed in KIR2DL1 despite the existence of conserved hydrophobic residues near the hinge region. |
| T7 |
1041-1194 |
Sentence |
denotes |
There is also a 5 degrees difference in the observed hinge angles in two crystal forms of 2DL2, suggesting that the interdomain hinge angle is not fixed. |
| T8 |
1195-1345 |
Sentence |
denotes |
The putative ligand-binding site is formed by residues from several variable loops with charge distribution apparently complementary to that of HLA-C. |
| T9 |
1346-1480 |
Sentence |
denotes |
The packing of the receptors in the orthorhombic crystal form offers an intriguing model for receptor aggregation on the cell surface. |
