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Article

Double domain swapping in bovine seminal RNase: formation of distinct N- and C-swapped tetramers and multimers with increasing biological activities.

PloS one - 1 Jan 2012

Gotte Giovanni, Mahmoud Helmy Alexander, Ercole Carmine, Spadaccini Roberta, Laurents Douglas V, Donadelli Massimo, Picone Delia

Abstract excerpt

Bovine seminal (BS) RNase, the unique natively dimeric member of the RNase super-family, represents a special case not only for its additional biological actions but also for the singular features of 3D domain swapping. The native enzyme is indeed a mixture of two isoforms: M = M, a dimer held together by two inter-subunit disulfide bonds, and MxM, 70% of the total, which, besides the two mentioned disulfides, is...

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PMID: 23071641
DOI: 10.1371/journal.pone.0046804
PMCID: PMC3469567

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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