By Frank J. Dixon (Ed.)
With contributions from Steven A. Porcelli and different the world over famous leaders within the box, this quantity keeps the culture of vital studies. Papers at the CD1 kinfolk, confident choice of thymocytes, and molecular and mobile facets of XLA spotlight the newest quantity.
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Additional info for Advances in Immunology, Vol. 59
C)Alignment of human CD1 a3 consensus sequence with a3 (CMV H301, FcRn, MICA, HLA-F, and HLA-A2), a2 (HLA-DRa, HLA-DMA), or j32 (HLA-DW, HLA-DMB) domains of other proteins. The human CD1 consensus sequences are derived from the alignment of the five human CD1 proteins shown in Fig. 3. Consensus residues indicate the most common amino acid occurring at each position. An X denotes that no residue occurs more than once at that position. Alignments were performed as described in the legend to Fig.
Although the accuracy of such methods is questionable in the absence of supportive experimental data, these findings at least raise the possibility that the a1 and a2 domains of CD1 may not fold into a structure that closely resembles the peptidebinding groove of MHC class I or I1 molecules. 9. Secondary structure predictions for the a 2 domains of CD1 proteins. The scale indicates the amino acid position, starting from the first N-terminal residue of the a2 domains. Filled boxes indicate predicted 8 strands of 8-pleated sheet structure, and hatched boxes indicate predicted a-helical regions.
However, analysis of CDla purified from the MOLT-4 T leukemia cell line shows a molecular mass approximately 3 kDa greater than that of thymocyte CDla, and this difference persists after neuraminidase treatment (Van Agthoven and Terhorst, 1982). This was interpreted to be evidence of an additional oligosaccharide group on CD l a expressed by this tumor cell line. Since only four sites for Nlinked glycan attachment are predicted by the protein sequence of CDla, this may indicate the attachment of an 0-linked glycan in this case.