Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues
Crystal structures of two I-Ad-peptide complexes reveal that high affinity can be achieved without large anchor residues
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DOI：
10.1016/s1074-7613(00)80537-3
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发表时间：
1998-03-01
期刊：
影响因子：
32.4
通讯作者：
Wilson, IA
中科院分区：
文献类型：
--
作者：
Scott, CA;Peterson, PA;Wilson, IA
我们已经确定了与卵清蛋白肽（OVA（323-339））和流感病毒血凝素肽（HA（126-138））共价连接的I-A（d）的结构。肽结合沟的底部含有不寻常的β凸起，在I-E和DR结构中看不到，其影响α和β链与结合肽之间的许多相互作用。与其它MHC-肽复合物不同，所述肽不将任何大的锚残基插入浅I-A（d）结合沟的结合口袋中。先前鉴定的I-A（d）的六残基“核心”结合基序仅占据P4至P9口袋，这意味着I-A（d）-肽复合物的T细胞受体识别的特异性可以通过仅部分填充MHC沟的肽来实现。
We have determined the structures of I-A(d) covalently linked to an ovalbumin peptide (OVA(323-339)) and to an influenza virus hemagglutinin peptide (HA(126-138)). The floor of the peptide-binding groove contains an unusual beta bulge, not seen in I-E and DR structures, that affects numerous interactions between the alpha and beta chains and bound peptide. Unlike other MHC-peptide complexes, the peptides do not insert any large anchor residues into the binding pockets of the shallow I-A(d) binding groove. The previously identified six-residue "core" binding motif of I-A(d) occupies only the P4 to P9 pockets, implying that specificity of T cell receptor recognition of I-A(d)-peptide complexes can be accomplished by peptides that only partially fill the MHC groove.