Sterkers G, Tiercy J M, Zeliszewski D, Levy J P, Mach B
Laboratoire d'Immunologie et d'Oncologie des Maladies Rétrovirales, INSERM U 152, CNRS UA 628, Hôpital Cochin, Paris, France.
Eur J Immunol. 1989 Sep;19(9):1585-90. doi: 10.1002/eji.1830190910.
An HLA-DR product encoded by the HLA-DRw13/Dw19 haplotype has been identified as the HLA class II molecule involved in antigen presentation to several influenza-specific helper T cell clones. Three different functional sites were identified on this molecule by comparing the structure of HLA-DR products of known sequences and their ability to efficiently present foreign antigen to the T cell clones. These functional sites were mapped on the recently proposed three-dimensional structure of HLA class II molecules. From their position, these sites are all potentially involved in HLA-peptide interaction and capable of affecting the binding and/or the conformation of the foreign peptide. This suggests that polymorphic residues essential in major histocompatibility complex restriction are mostly involved in peptide binding.
由HLA - DRw13/Dw19单倍型编码的一种HLA - DR产物已被确定为参与向多个流感特异性辅助性T细胞克隆呈递抗原的HLA II类分子。通过比较已知序列的HLA - DR产物的结构及其向T细胞克隆有效呈递外来抗原的能力,在该分子上确定了三个不同的功能位点。这些功能位点被定位到最近提出的HLA II类分子的三维结构上。从它们的位置来看,这些位点都可能参与HLA - 肽相互作用,并能够影响外来肽的结合和/或构象。这表明在主要组织相容性复合体限制中至关重要的多态性残基大多参与肽的结合。