id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-299279-v0vznri2	Røder, Gustav	Structure of a SARS coronavirus-derived peptide bound to the human major histocompatibility complex class I molecule HLA-B*1501	2008-05-17		.txt	text/plain	2815	178	68	The peptide is deeply anchored in the B and F pockets, but with the Glu4 residue pointing away from the floor in the peptide-binding groove, making it available for interactions with a potential T-cell receptor. The overall structure of the present HLA-B*1501 peptide-binding groove is similar to the previously two determined HLA-B*1501 structures (Røder et al., 2006) and to other MHC-I molecules (see Fig. 1 ). The pGln2 peptide residue is located in the B pocket in the same orientation as the pGlu2 in the previously described HLA-B*1501-LEKARGSTY structure (Røder et al., 2006) . The pGlu4 peptide residue points away from the peptide-binding groove and the side chain does not interact with any HLA-B*1501 residues. The conformation observed does not interact with any HLA-B*1501 residues, but makes a hydrogen bond to two water molecules (HOH67 and HOH348) present between the peptide and the floor of the peptide-binding groove, thereby forming water-mediated contacts with the HLA-B*1501 protein.	./cache/cord-299279-v0vznri2.txt	./txt/cord-299279-v0vznri2.txt