The jelly roll or Swiss roll fold is a protein fold or supersecondary structure composed of eight beta strands arranged in two four-stranded sheets. The name of the structure was introduced by Jane S. Richardson in 1981, reflecting its resemblance to the jelly or Swiss roll cake.[2] The fold is an elaboration on the Greek key motif and is sometimes considered a form of beta barrel. It is very common in viral proteins, particularly viral capsid proteins.[3][4] Taken together, the jelly roll and Greek key structures comprise around 30% of the all-beta proteins annotated in the Structural Classification of Proteins (SCOP) database.[5]
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- ^ Richardson JS (1981). "The anatomy and taxonomy of protein structure". Advances in Protein Chemistry Volume 34. Vol. 34. pp. 167–339. doi:10.1016/S0065-3233(08)60520-3. ISBN 9780120342341. PMID 7020376.
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- ^ Cheng S, Brooks CL (7 February 2013). "Viral capsid proteins are segregated in structural fold space". PLOS Computational Biology. 9 (2): e1002905. Bibcode:2013PLSCB...9E2905C. doi:10.1371/journal.pcbi.1002905. PMC 3567143. PMID 23408879.
- ^ Edwards H, Abeln S, Deane CM (14 November 2013). "Exploring fold space preferences of new-born and ancient protein superfamilies". PLOS Computational Biology. 9 (11): e1003325. Bibcode:2013PLSCB...9E3325E. doi:10.1371/journal.pcbi.1003325. PMC 3828129. PMID 24244135.