Affiliations: CNR, Ctro. di Stud. di B., Universita Federico II di Napoli, Via Mezzocannone 4, 80134 Napoli, Italy
Dipto. di Chim. Organica e Biologica, Universita Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy
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BS-RNase tetramers: An example of domain-swapped oligomers
In the ribonuclease superfamily, dimericity is a unique feature of bovine seminal RNase (BS-RNase). In about two-thirds of native BS-RNase molecules, the two subunits interchange their N-terminal tails, thus generating domain-swapped dimers (MxM), which mostly responsible for enzyme biological activities and allostericity. Higher molecular weight BS-RNase oligomers can also be prepared [Libonati, M. (1969) Ital. J. Biochem. 18, 407-417.]. This paper reports on BS-RNase tetrameric derivatives which were isolated and enzymatically characterized. The data collected and the analysis of the crystal packing of MxM dimers suggested a structural model for tetramer assembly, in which the four subunits are enchained by multiple domain-swapping events.
BS-RNase tetramers: An example of domain-swapped oligomers
No results.
BS-RNase tetramers: An example of domain-swapped oligomers
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