Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pill strains PAO, KB7, and PAK: Implications for receptor binding and synthetic vaccine design
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pill strains PAO, KB7, and PAK: Implications for receptor binding and synthetic vaccine design
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DOI：
10.1021/bi00050a005
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发表时间：
1995-12-19
期刊：
影响因子：
2.9
通讯作者：
Sykes, BD
中科院分区：
文献类型：
--
作者：
Campbell, AP;McInnes, C;Sykes, BD
用二维H-1核磁共振技术测定了铜绿假单胞菌PAO和Kb7菌株受体结合区的多肽抗原的溶液结构。使用模拟退火法结合从核磁共振数据得到的距离和扭角约束，生成了这些17个残基二硫键桥联多肽反式的溶液构象系综。将PAO和Kb7多肽的核磁共振衍生溶液结构与先前确定的(McInnes等人，1993)进行比较，并在此提炼出PAK多肽，揭示了一个共同的结构基序。这三种多肽结构都含有保守序列Asp(134)-X-X-Phe(137)中的I型β-转角和保守序列Pro(139)-X-Gly-Cys(142)中的II型β-转角。然而，这三种多肽的整体折叠以及组成疏水口袋的侧链的配置都不同。根据它们对合成疫苗设计的贡献，讨论了与共同细胞表面受体结合的三种毒株的结构之间的异同。
The solution structures of peptide antigens from the receptor binding domains of Pseudomonas aeruginosa strains PAO and KB7 have been determined using two-dimensional H-1 NMR techniques. Ensembles of solution conformations for the trans forms of these 17-residue disulfide-bridged peptides have been generated using a simulated annealing procedure in conjunction with distance and torsion angle restraints derived from NMR data. Comparison of the NMR-derived solution structures of the PAO and KB7 peptides with that previously determined (McInnes er al., 1993) and herein refined for the PAK peptide reveals a common structural motif. All three peptide structures contain a type I beta-turn in the conserved sequence Asp(134)-X-X-phe(137) and a type II beta-turn in the conserved sequence Pro(139)-X-Gly-Cys(142). However the overall folds of the three peptides differ as well as the disposition of the side chains comprising the hydrophobic pockets. The similarities and differences between the structures of the three strains which bind to a common cell surface receptor are discussed in light of their contributions to synthetic vaccine design.