Tripp Timothy J, McCormick John K, Webb Jennifer M, Schlievert Patrick M
Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USA.
Infect Immun. 2003 Mar;71(3):1548-50. doi: 10.1128/IAI.71.3.1548-1550.2003.
The cocrystal structure of streptococcal pyrogenic exotoxin C (SPE C) with HLA-DR2a (DRA0101,DRB50101) revealed a zinc-dependent interaction site through residues 167, 201, and 203 on SPE C and residue 81 on the beta-chain of HLA-DR2a (DRA0101,DRB50101). Mutation of these SPE C residues resulted in dramatically reduced biological activities. Thus, the zinc-dependent major histocompatibility complex II binding site is critical for maximal biological function of SPE C.
链球菌致热外毒素C(SPE C)与HLA - DR2a(DRA0101,DRB50101)的共晶体结构揭示了一个锌依赖性相互作用位点,该位点通过SPE C上的167、201和203位残基以及HLA - DR2a(DRA0101,DRB50101)β链上的81位残基形成。这些SPE C残基的突变导致生物活性显著降低。因此,锌依赖性主要组织相容性复合体II结合位点对SPE C的最大生物学功能至关重要。