Dynamic Interaction among the Platform Domain and Two Membrane-Proximal Immunoglobulin-Like Domains of Class I Major Histocompatibility Complex : Normal Mode Analysis

概要

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Class I major histocompatibility complex (MHC) molecules have three domains, a platform domain and two membrane-proximal immunoglobulin-like domains, an α3 domain and a β_2-immunoglobulin (β_2m). To understand the dynamic interactions among the three domains, we simulated the behavior of a partial model deficient in β_2m and another model deficient in the α3 domain, by normal mode analysis. As a result, the partial model deficient in β_2m was more flexible in interdomain conformation than the other model. The lowest frequency modes (<2 cm^<-1>) observed for the simulations of the partial model deficient in β_2m showed clear interdomain motions as if each domain moved like a rigid body. Such low frequencies and clear interdomain motions were not observed for the simulations of the other model, therefore the interdomain flexibility of the partial model deficient in β_2m may be due to the lowest frequency modes (<2 cm^<-1>). These results suggest that β_2m contributes to maintaining the interdomain conformation of class I MHC molecules more than the α3 domain does, and may offer convincing evidence to support the notion that the α3 domain and β_2m do not have an equal influence on the structural stability of class I MHC molecules.
社団法人日本薬学会の論文
2008-05-01