Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase
Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase(1300 views) Pica A, Merlino A, Buell AK, Knowles TJ, Pizzo E, D'Alessio G, Sica F, Mazzarella L
Keywords: Atomic Force Microscopy, Fibril Formations, Ribonuclease, Supramolecular Aggregates, Three-Dimensional Domain Swapping, Pancreatic Ribonuclease, Article, Chemistry, Fluorometry, Gene Deletion, Genetic Variability, Human, Methodology, Predictive Value, Protein Engineering, Protein Folding, Protein Multimerization, Protein Tertiary Structure, Ultrastructure, X Ray Crystallography, X-Ray, Genetic Variation, Predictive Value Of Tests, Protein Structure,
Affiliations: *** IBB - CNR ***
Department of Chemical Sciences, University of Naples 'Federico II', Via Cintia, 80126 Naples, Italy
Institute of Biostructures and Bioimages, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Department of Structural and Functional Biology, University of Naples 'Federico II', Via Cintia, 80126 Naples, Italy
References: Not available.
Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase
The deletion of five residues in the loop connecting the N-terminal helix to the core of monomeric human pancreatic ribonuclease leads to the formation of an enzymatically active domain-swapped dimer (desHP). The crystal structure of desHP reveals the generation of an intriguing fibril-like aggregate of desHP molecules that extends along the c crystallographic axis. Dimers are formed by three-dimensional domain swapping. Tetramers are formed by the aggregation of swapped dimers with slightly different quaternary structures. The tetramers interact in such a way as to form an infinite rod-like structure that propagates throughout the crystal. The observed supramolecular assembly captured in the crystal predicts that desHP fibrils could form in solution; this has been confirmed by atomic force microscopy. These results provide new evidence that three-dimensional domain swapping can be a mechanism for the formation of elaborate large assemblies in which the protein, apart from the swapping, retains its original fold.
Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase
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Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase