Buxton S E, Benjamin R J, Clayberger C, Parham P, Krensky A M
Department of Pediatrics, Stanford University Medical Center, California 94305.
J Exp Med. 1992 Mar 1;175(3):809-20. doi: 10.1084/jem.175.3.809.
Dissection of the peptide binding grooves of seven subtypes of human histocompatibility leukocyte antigen (HLA)-B27 into the six specificity pockets defined by the 2.6-A structure of HLA-A0201 revealed just one pocket, the B ("45") pocket, that is conserved among all the HLA-B27 subtypes. Functional studies of mutant HLA-B2705 molecules with point substitutions in residues of the B pocket show that this structure, and the glutamine residue at position 45 in particular, plays a critical role in cell surface expression, peptide binding, and in the presentation of both exogenous and endogenous peptides by HLA-B2705. We predict that the B pocket of HLA-B2705 interacts with an amino acid side chain that anchors peptides in the binding groove, and that this peptide motif is present in most endogenously processed peptides that bind to all seven subtypes of HLA-B27.
将人类组织相容性白细胞抗原（HLA）-B27的七个亚型的肽结合凹槽解析为HLA-A0201的2.6埃结构所定义的六个特异性口袋，结果显示只有一个口袋，即B（“45”）口袋，在所有HLA-B27亚型中是保守的。对B口袋残基进行点突变的突变型HLA-B2705分子的功能研究表明，该结构，特别是45位的谷氨酰胺残基，在细胞表面表达、肽结合以及HLA-B2705对外源和内源性肽的呈递中起关键作用。我们预测，HLA-B2705的B口袋与一个将肽锚定在结合凹槽中的氨基酸侧链相互作用，并且该肽基序存在于大多数与HLA-B27的所有七个亚型结合的内源性加工肽中。
