Harris P E, Colovai A, Liu Z, Dalla Favera R, Suciu-Foca N
Division of Immunogenetics, College of Physicians and Surgeons of Columbia University, New York, NY 10032.
J Immunol. 1993 Dec 1;151(11):5966-74.
Naturally processed peptides, bound to HLA-A2, A68, B40 molecules, were isolated from a c-myc transfected lymphoblastoid B cell lines for sequence analysis. Forty-three sequences of bound peptides could be grouped into three structural motifs. One of the peptide sequences obtained, SLLPAIVEL, was identical to a previously reported peptide bound to HLA-A2.1 and was used for grouping HLA-A2-bound peptides. A second motif, identical to that previously reported for HLA-A68-bound peptides, was also observed. A distinct third motif, consistent with the structure of the HLA-B40 "45 pocket," was observed. The peptides within this group contained glutamate in position 2, usually followed by a hydrophobic residue in positions 3 and 9. Within this motif group of peptides bound to MHC class I molecules, one peptide, HEETPPTTS, was 100% homologous to residues 243-251 of the c-myc protein.
从转染了c-myc的淋巴母细胞样B细胞系中分离出与HLA-A2、A68、B40分子结合的天然加工肽，用于序列分析。43个结合肽序列可分为三种结构基序。获得的一个肽序列SLLPAIVEL与先前报道的与HLA-A2.1结合的肽相同，用于对与HLA-A2结合的肽进行分组。还观察到了与先前报道的与HLA-A68结合的肽相同的第二个基序。观察到一个独特的第三个基序，与HLA-B40“45口袋”的结构一致。该组中的肽在第2位含有谷氨酸，通常在第3位和第9位之后接着一个疏水残基。在与MHC I类分子结合的该基序组肽中，一个肽HEETPPTTS与c-myc蛋白的243-251位残基100%同源。
