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55 Years of the Rossmann Fold

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Protein Supersecondary Structures

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1958))

Abstract

The Rossmann fold is one of the most commonly observed structural domains in proteins. The fold is composed of consecutive alternating β-strands and α-helices that form a layer of β-sheet with one (or two) layer(s) of α-helices. Here, we will discuss the Rossmann fold starting from its discovery 55 years ago, then overview entries of the fold in the major protein classification databases, SCOP and CATH, as well as the number of the occurrences of the fold in genomes. We also discuss the Rossmann fold as an interesting target of protein engineering as the site-directed mutagenesis of the fold can alter the ligand-binding specificity of the structure.

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Acknowledgments

The authors are thankful for Lyman Monroe for proofreading the manuscript. This work was partly supported by the National Institute of General Medical Sciences of the NIH (R01GM123055) and the National Science Foundation (DMS1614777, CMMI1825941).

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Authors and Affiliations

  1. Department of Biological Science, Purdue University, West Lafayette, IN, USA

    Woong-Hee Shin & Daisuke Kihara

  2. Department of Computer Science, Purdue University, West Lafayette, IN, USA

    Daisuke Kihara

Authors
  1. Woong-Hee Shin
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  2. Daisuke Kihara
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Corresponding author

Correspondence to Daisuke Kihara .

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Editors and Affiliations

  1. Department of Mathematics, Rutgers University, Piscataway, NJ, USA

    Alexander E. Kister

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Shin, WH., Kihara, D. (2019). 55 Years of the Rossmann Fold. In: Kister, A. (eds) Protein Supersecondary Structures. Methods in Molecular Biology, vol 1958. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9161-7_1

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  • DOI: https://doi.org/10.1007/978-1-4939-9161-7_1

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-9160-0

  • Online ISBN: 978-1-4939-9161-7

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