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Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization

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  • Masayuki Yamasaki

    (University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK)

  • Wei Li

    (University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK)

  • Daniel J. D. Johnson

    (University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK)

  • James A. Huntington

    (University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK)

Abstract

The molecular basis of serpin polymerization The serpins are a family of proteins that can multimerize via β-sheet linkages. Accumulation of such multimers can give rise to diseases such as thrombosis, cirrhosis and dementia. While the structures of many serpins are known, the structure of the linkage between monomers was unclear. In this work, Huntington and colleagues have solved the crystal structure of an antithrombin dimer. They find that the high stability of the serpin polymer is due to a large domain swap between beta sheets of the neighbouring monomers. In addition, the structure explains the how certain pathogenic mutations stabilize a polymerogenic folding intermediate.

Suggested Citation

  • Masayuki Yamasaki & Wei Li & Daniel J. D. Johnson & James A. Huntington, 2008. "Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization," Nature, Nature, vol. 455(7217), pages 1255-1258, October.
    • Handle: RePEc:nat:nature:v:455:y:2008:i:7217:d:10.1038_nature07394
    DOI: 10.1038/nature07394
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    Cited by:

    1. Atul Kumar Upadhyay & Ramanathan Sowdhamini, 2016. "Genome-Wide Prediction and Analysis of 3D-Domain Swapped Proteins in the Human Genome from Sequence Information," PLOS ONE, Public Library of Science, vol. 11(7), pages 1-20, July.

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