Open AccessPrimary structure of murine major histocompatibility complex alloantigens: Amino acid sequence studies of the cyanogen bromide fragments of the H-2K b glycoprotein
Author(s) -
John E. Coligan,
Thomas J. Kindt,
Bruce M. Ewenstein,
Hiroshi Uehara,
Tosiki Nisizawa,
Stanley G. Nathenson
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.7.3390
Subject(s) - cyanogen bromide , major histocompatibility complex , peptide sequence , homology (biology) , amino acid , protein primary structure , glycoprotein , histocompatibility , stereochemistry , microbiology and biotechnology , biology , molecule , chemistry , sequence (biology) , gene , biochemistry , genetics , antigen , human leukocyte antigen , organic chemistry
Radiochemical microtechniques have been used in the amino acid sequence analysis of five major CNBr fragments of the glycoprotein specified by the murine major histocompatibility complex geneH-2k b . These fragments have been tentatively aligned and represent the NH2 -terminal 80% of the intact molecule. All amino acids except Asp, Asn, and Gln have been assigned in 128 out of 149 possible positions in the NH2 -terminal portions of each of these fragments. These assignments, which represent approximately 50% of the total sequence from these fragments, are listed below in the order of their alignment in the intact H-2Kb molecule: IIIn, -PHSLRYFVTAVSRP(G)L(G)(E)PRYM; IIIa, EVGYV--TEFVRF-S-AE(A)PRYEPR(A)--M; Ib, E-EGPEYWERET-KAK(G)-E-SFR--LRTLL(G)YY--TK; Ia, AALITK-KWE-AGEAERLRAYLEGTC-E-L; Ic, ELVETRPAG-GTF-KWAS-VVPLGKE-YY(T). The unassigned positions represented by dashes in the above sequences may be tentatively assigned as Asp, Asn, or Gln.The NH2 -terminal sequence obtained for the H-2Kb molecule was compared to the limited sequence information available for other major histocompatibility complex gene products. An 84% homology (16 of 19 residues) to the H-2Kq and H-2Kk molecules, which are identical to one another in the positions compared, was observed. A similar comparison with 28 of the 31 NH2 -terminal residues of HLA-B7 indicated 68% homology. Furthermore, significant homology was observed between H-Kb and HLA-B7 in a region of glycosylation, which occurs between positions 85 and 100 in the two molecules.