Article Abstract:
The 3-D structure of the class II glycoprotein HLA-DRI, analogous to that of class I HLA, is characterized by two alpha-chain domains and two beta-chain domains. Eight strands of antiparallel beta-sheet forming the floor and two anti-parallel helical regions as the sides constitute the peptide-binding groove of both the class I and II of HLA-DRI. The binding site for a peptide 'anchor' side chain in DRI is a deep pocket surrounded by non-polar residues of alpha and beta chains. The presence of the alphabeta heterodimers of class II DRI in the crystal forms of HLA-DRI implies the possibility of dimerization starting a cytoplasmic signalling for activating the T cells.
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Article Abstract:
The atomic arrangement of the peptide group HLA-Aw68 has been verified at the 1.9 Angstrom level from X-ray diffraction analysis of a peptide crystal at -165 degrees Celsius. The HLA-Aw68 peptides are of varying lengths and are linked together at the ends but not in the central region. This new insight into peptide structure may elucidate how they succeed in attaching to the class I histocompatibility glycoproteins as a part of the immune response.
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Article Abstract:
Acid-eluted peptides bound to HLA-DR1 have a heterogeneously-sized structure obtained from endogenously synthesized proteins, especially the major histocompatibility complex-related proteins. The peptides' complete sequence data were determined using high-performance liquid chromatography, mass spectrometry and microsequencing analysis. Particular amino acids in the HLA-DR-beta-chains probably determine allelic specificity of peptide binding.
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