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NMR of modular proteins

Nature Structural Biology volume 5, pages 496–499 (1998)Cite this article

Abstract

NMR studies of domains, dissected from large modular proteins, are described. Particular emphasis is placed on modules from the extracellular proteins fibrillin-1 and fibronectin.

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Figure 1: Module organization of fibrillin-110 and fibronectin8.
Figure 2: Multiple sequence alignment of TB modules from human fibrillin-1.
Figure 3: Superposition of the TB6 family of NMR structures14.
Figure 4: Schematic ribbon drawing of fibrillin cbEGF 32–3317.
Figure 5: The structure of a pair of fibronectin F3 modules (from coordinates of Leahy et al.16).

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Acknowledgements

Acknowledgments

A.K.D. thanks the Wellcome Trust and The Queen's College, Oxford for support. I.D.C. is also supported by the Wellcome Trust. The authors acknowledge P. Handford for critical reading of the manuscript. The Oxford Centre for Molecular Sciences is funded by the Biology and Biotechnology Sciences Research Council, Engineering and Physical Sciences Research Council and Medical Research Council.

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Authors and Affiliations

  1. Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, England

    Iain D. Campbell & A. Kristina Downing

  2. Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, England

    Iain D. Campbell & A. Kristina Downing

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Correspondence to Iain D. Campbell.

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Campbell, I., Downing, A. NMR of modular proteins. Nat Struct Mol Biol 5 (Suppl 7), 496–499 (1998). https://doi.org/10.1038/733

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