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Comparison of four independently determined structures of human recombinant interleukin–4

Nature Structural Biology volume 1, pages 301–310 (1994)Cite this article

Abstract

Four independent structures of human interleukin–4, two determined by nuclear magnetic resonance techniques and two by X–ray diffraction, have been compared in detail. The core of this four helix bundle protein is very similar in all the structures but there are some differences in loop regions that are known to be mobile in solution. Careful comparison of the experimental data sets and the methods of analysis of the different laboratories has provided clues to the sources of most of the differences, and also answered some general questions about the accuracy of protein structure determination by these two techniques.

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Authors and Affiliations

  1. Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, UK

    Lorna J. Smith, Christina Redfield & Christopher M. Dobson

  2. SmithKline Beecham Pharmaceuticals, The Pinnacles, ColdharbourRoad, Harlow, Essex., UK

    Richard A. G. Smith

  3. Laboratory of Chemical Physics, Building 2, National Institute for Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, 20892, USA

    G. Marius Clore & Angela M. Gronenborn

  4. Department of Pharmacology, University of Alabama at Birmingham, UAB station, Birmingham, Alabama, 35294, USA

    Mark R. Walter

  5. Schering-Plough Research Institute, Bloomfield, New Jersey, 07003, USA

    Tattanahalli L. Naganbushan

  6. Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, ABL-Basic Research Program, Frederick, MD, 21702, USA

    Alexander Wlodawer

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  1. Lorna J. Smith
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  9. Alexander Wlodawer
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Smith, L., Redfield, C., Smith, R. et al. Comparison of four independently determined structures of human recombinant interleukin–4. Nat Struct Mol Biol 1, 301–310 (1994). https://doi.org/10.1038/nsb0594-301

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