| First Author | Zhu Y | Year | 2003 |
| Journal | J Mol Biol | Volume | 326 |
| Issue | 4 | Pages | 1157-74 |
| PubMed ID | 12589760 | Mgi Jnum | J:230358 |
| Mgi Id | MGI:5758811 | Doi | 10.1016/s0022-2836(02)01437-7 |
| Citation | Zhu Y, et al. (2003) Crystal structure of MHC class II I-Ab in complex with a human CLIP peptide: prediction of an I-Ab peptide-binding motif. J Mol Biol 326(4):1157-74 |
| abstractText | Association between the class II major histocompatibility complex (MHC) and the class II invariant chain-associated peptide (CLIP) occurs naturally as an intermediate step in the MHC class II processing pathway. Here, we report the crystal structure of the murine class II MHC molecule I-A(b) in complex with human CLIP at 2.15A resolution. The structure of I-A(b) accounts, via the peptide-binding groove's unique physicochemistry, for the distinct peptide repertoire bound by this allele. CLIP adopts a similar conformation to peptides bound by other I-A alleles, reinforcing the notion that CLIP is presented as a conventional peptide antigen. When compared to the related HLA-DR3/CLIP complex structure, the CLIP peptide displays a slightly different conformation and distinct interaction pattern with residues in I-A(b). In addition, after examining the published sequences of peptides presented by I-A(b), we discuss the possibility of predicting peptide alignment in the I-A(b) binding groove using a simple scoring matrix. |
