Primary structure of murine major histocompatibility alloantigens: amino acid sequence of the cyanogen bromide fragment Ia (positions 139-228) from the H-2Kb molecule.
Primary structure of murine major histocompatibility alloantigens: amino acid sequence of the cyanogen bromide fragment Ia (positions 139-228) from the H-2Kb molecule.
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鼠主要组织相容性同种抗原的一级结构:H-2Kb 分子的溴化氰片段 Ia(位置 139-228)的氨基酸序列。
DOI:
10.1021/bi00567a036
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发表时间:
1980
期刊:
影响因子:
2.9
通讯作者:
Coligan,JE
中科院分区:
文献类型:
--
作者:
Uehara,H;Ewenstein,BM;Martinko,JM;Nathenson,SG;Kindt,TJ;Coligan,JE
Lancet, D., & Strominger, J. L.(1979) Biochemistry 18, 5711] is 68%, and differences are noted at positions 176, 177, and 178 which in the H-2 molecule are the attachment region for a second carbohydrate moiety. No carbohydrate was detected in this position forHLA-B7 [Orr,. T. Lopez de Castro, J. A. Lancet, D., & Strominger, J. L.(1979) Biochemistry 18, 5711], e classical histocompatibility antigens are the products of the polymorphic genes at the K, D, and L regions of the murine H-2 major histocompatibility complex (MHC) 1 [see reviews by Klein (1975, 1979), Snell et al.(1976), and Vitetta & Capra (1978)]. These products are integral cell surface glycoproteins containing~ 340 amino acids (Schwartz et al., 1973), and they exist in the membrane in association with ß2-microglobulin, a polypeptide of molecular weight 12000 (Rask et al., 1974; Silver & Hood, 1974; Natori et al., 1975). Although the primary function of these antigenic products remains obscure, recent data suggest that they play a role in the recognition of virally induced and other cell surface an-tigens, in a process termed “associative recognition”[see re-views by Paul & Benacerraf (1977), Shearer & Schmitt-Verhulst (1977), and Zinkernagel & Doherty (1979)]. Possibly related to their postulated role in cell recognition is the remarkable polymorphism of the K and D gene products, a property first discovered in early serological analysis of