PRESENTATION OF N-FORMULATED PEPTIDES BY H2-M3
PRESENTATION OF N-FORMULATED PEPTIDES BY H2-M3
复制标题
DOI：
10.1042/bst0230669
复制
发表时间：
1995-08-01
影响因子：
3.9
通讯作者：
WANG, CR
中科院分区：
文献类型：
--
作者：
LINDAHL, KF;DABHI, VM;WANG, CR
与经典的I类基因一样，H2-M3在胚胎生命的第8天之前表达，并且其表达可由γ-干扰素诱导[15]。M3转录本在北方印迹中易于检测，其水平约为总I类mRNA的1/20 [3]。胸腺中的水平最高，其次是肝脏、肾脏和脾脏;睾丸中几乎检测不到mRNA，大脑中根本检测不到。M3与经典的MHC I类基因Ld的核苷酸相似性范围为外显子2的69%至外显子4的86%。M3和许多Ia类分子的胞外结构域具有相同的长度，并且共享大多数通常保守的残基，例如半胱氨酸和残基86处的糖基化位点。M3蛋白具有全长的疏水性跨膜结构域和8个氨基酸的亲水性锚。M3与其他I类分子最显著的不同之处在于没有指向肽结合位点的带电残基。
Like classical class I genes, H2-M3 is expressed from before day 8 of embryonic life, and its expression is inducible with y-interferon [15]. M3 transcripts are readily detectable in a Northern blot, at a level about 1/20 of total class I mRNA [3]. The highest levels are in thymus, followed by liver, kidney and spleen; the mRNA is barely detectable in testis and not at all in brain. The nucleotide similarity of M3 to Ld, a classical MHC class I gene, ranges from 69% in exon 2 to 86% in exon 4. The extracellular domains of M3 and many class Ia molecules have the same length and share the majority of generally conserved residues, such as cysteiries and the glycosylation site at residue 86. The M3 protein has a full-length, hydrophobic transmembrane domain and an eight-amino-acid hydrophilic anchor. M3 differs most notably from other class I molecules by the absence of charged residues pointing into the peptide-binding site.