The phylogenetic tree signaling pathway also showed that three SLA-2-HB alleles were close to SLA-2*10es21, SLA-2*1001, SLA-2*10sk21 and SLA-2*10sm01

(Fig. However, all SLA-2 alleles were different from HLA-A2 with at least 0.336 distances. The SLA-2-HB alleles were aligned with representative rat and human MHC class I alleles and the main variable amino acids in their functional domains analyzed. The results are shown in Figure 2. In the signal peptide domain, the SLA-2-HB alleles differed from H-2K1, HLA-B15 and HLA-A2; the numbers of different amino acids were 14, 8 and 10, respectively. In the α1 and α2 domain in which the peptide-binding groove is located, SLA-2-HB retained all eight key amino acids that can bind Selleckchem MK1775 peptides in human HLA-A2; that is Y7, Y59, Y84, T143, K146, W147, Y159 and Y171 (11). SLA-2-HB retained 14 of the 19 amino acids in the α1 and α2 domains of HLA-A2 that bind β2m. It was also found that the extracellular domain of SLA-2-HB contained three key amino acids, Gln115(Q), Asp122(D) and Glu128(E), that bind CD8 molecules (12). SLA-2-HB retained 18 of the CD8-binding amino acids at sites 199–223 of the α3 domain; seven amino acids had mutated, at 199(V/A), 207(G/S), 211(K/A), 214(S/T), 216(S/T), 220(E/D) and 222(Q/E) Comparing SLA-2-HB with H-2K1 and HLA-B15, the number of mutated amino acids was eight and six,

respectively. It has been reported that 199–205, 211 and 221 are the essential amino acid sites for binding CD8 molecules (13,14), and SLA-2-HB had mutated at 199(V/A) and 211(K/A). Compared with H-2K1, SLA-2-HB had mutated at site 211(K/A); compared with HLA-B15, the variable sites were 199(V/A) and 211(K/A). SLA-2-HB showed complete consistence with the amino acids that

bind β2m in the α3 domain of HLA-A2. SLA-2-HB displayed more variable amino acid sites with HLA-A2, H-2K1 and HLA-B-15 cytoplasmic and transmembrane domains than in other domains. The homology modeling of SLA-2-HB01 as well as SLA-2-HB02, SLA-2-HB03 and SLA-2-HB04 showed a very similar 3D structure, i.e, with two α-Helix structure and eight β-strain structure, Liothyronine Sodium which constituted an antigenic peptides groove of SLA-2 protein. Most of the 11 key variable amino acid sites were found in the antigenic peptides groove of SLA-2 protein. Among them, 73(N), 155(G), 156(E) sites were in α-helical regions while 23(F), 24(I), 95(I), 114(R), and 216(S) sites were all in β-strain regions, and only 43(A), 44(K), 50(Q), sites were outside of antigenic peptides groove of SLA-2 protein (Fig. SLA-2 shows dissimilarity to the SLA-1 and SLA-3 alleles in three amino acids at the start of the signal peptide (6). Detailed genetic characteristics of SLA-2 locus have been reported, but the characteristics of SLA-2 from the Hebao pig in China have never been elucidated.