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Topology, sequence evolution and folding dynamics of an immunoglobulin domain

Nature Structural Biology volume 5, pages 194–198 (1998)Cite this article

Abstract

The pH-dependence of hydrogen-exchange, in native conditions, is used to probe the formation of secondary structure in the folding of an immunoglobulin domain (CD2.d1). The intermediate and transition states in the reaction are insensitive to pH, a simplification that allows us to equate structure formation and folding kinetics. The crucial residues in the folding reaction are grouped in the B, C, E and F strands which constitute a ‘crossover’ nucleus in the β-sandwich. These residues show the highest sequence conservation within the family of folds to which this domain belongs and are located in a unit of structure that is the most consistent topo-logical feature of the immunoglobulin family.

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Authors and Affiliations

  1. Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol, BS8 1TD, UK

    Martin J. Parker, Christopher E. Dempsey & Anthony R. Clarke

  2. Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Sheffield, S10 2UH, UK

    Laszlo L.P. Hosszu & Jonathan P. Waltho

Authors
  1. Martin J. Parker
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  2. Christopher E. Dempsey
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  3. Laszlo L.P. Hosszu
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  4. Jonathan P. Waltho
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  5. Anthony R. Clarke
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Correspondence to Martin J. Parker.

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Parker, M., Dempsey, C., Hosszu, L. et al. Topology, sequence evolution and folding dynamics of an immunoglobulin domain. Nat Struct Mol Biol 5, 194–198 (1998). https://doi.org/10.1038/nsb0398-194

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