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Molecular Biology of the Cell Vol. 11, 1499 1507, May 2000 The Micro?pillar Proteins MAGP-1 and Fibrillin-1 Form a Ternary Complex with the Chondroitin Sulfate Proteoglycan Decor in Barbara Cripples
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We showed here that this protein exhibits three distinct binding modes to HST-1, which may be due to its ability to bind at a specific hinge. The results show that, when bound, its interactions with HST-1 produce binding of this protein to the chondroitin sulfate protein decor in C. trachomas cytoplasm. In this study, using a chondroitin sulfate proteoglycan decor protein probe, we demonstrated that this protein-protein interaction is mediated exclusively through a hinge-binding mode of binding and has a unique molecular mechanism. It is hypothesized that this mechanism helps explain the unique binding interactions of other chondroitin sulfate proteins to CNT-6 and HST-1, whose binding modes of binding are not based on a hinge structure. The results of this study will aid in the understanding of the chondroitin sulfate proteoglycan structure, and will also provide a useful model to study the interaction of other chondroitin sulfate protein proteins, including those with different hinge geometry. Department of Cell Biology and Physiology, Washington University School of Medicine, St.

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