Kinetics and Thermodynamics of 2-Microglobulin Binding to the mg src="http://pubs.acs.org/images/gifchars/alpha.gif
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- 作者：Andrea M. Hebert ; Jason Strohmaier ; Mary C. Whitman ; Trina Chen ; Elena Gubina ; Dawn M. Hill ; Marc S. Lewis ; and Steven Kozlowski
- 刊名：Biochemistry
- 出版年：2001
- 出版时间：May 1, 2001
- 年：2001
- 卷：40
- 期：17
- 页码：5233 - 5242
- 全文大小：107K
- 年卷期：v.40,no.17(May 1, 2001)
- ISSN：1520-4995
文摘
The major histocompatibility complex (MHC) class I molecule plays a crucial role in cytotoxiclymphocyte function. Functional class I MHC exists as a heterotrimer consisting of the MHC class Iheavy chain, an antigenic peptide fragment, and 
mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2-microglobulin (mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m). mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m has been previously shownto play an important role in the folding of the MHC heavy chain without continued mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m association withthe MHC complex. Therefore, mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m is both a structural component of the MHC complex and a chaperone-like molecule for MHC folding. In this study we provide data supporting a model in which the chaperone-like role of mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m is dependent on initial binding to only one of the two mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m interfaces with class 1 heavychain. mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2-Microglobulin binding to an isolated mages/gifchars/alpha.gif" BORDER=0>3 domain of the class I MHC heavy chain accuratelymodels the biochemistry and thermodynamics of mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m-driven refolding. Our results explain a 1000-folddiscrepancy between mages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">2m binding and refolding of MHC1. The biochemical study of the individual domainsof complex molecules is an important strategy for understanding their dynamic structure and multiplefunctions.