Journal of the American Chemical Society · 2020 · 38 citations · 29 references
Life SciencesBiochemistryMolecular BiologyProtein FoldingStructural BiochemistryStructural BiologyMacromolecular AssemblyMacromolecular StructureProtein Complex AssemblyProtein Folding ThermodynamicsProtein OligomerizationProtein StructureMolecular Architecture Of CollagenProtein Structural AnalysisRational DesignSalt Bridge DesignSalt Bridge FormationSalt Bridge InteractionsSalt BridgesTriple Helix Structure
Nature uses salt bridges to control the folding and stability of many proteins, including collagen, the key structural protein in mammals. Here, we present an interstrand salt bridge between (4S)-aminoproline (Amp) and aspartic acid (Asp) that directs the composition and register-specific assembly of synthetic collagen heterotrimers. This Amp–Asp salt bridge allowed for the rational design of strands that fold into A2B and ABC-type heterotrimers with only three salt bridges per triple helix. Native ESI-MS and NMR spectroscopic analyses corroborated the specific assembly of the ABC heterotrimer.
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Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 Å Resolution
Jordi Bella, Mark Eaton, Barbara Brodsky et al. · Science · 1994 · 1.1K citations
Structural Basis of Collagen Recognition by Integrin α2β1
Jonas Emsley, Christopher G. Knight, Richard W. Farndale et al. · Cell · 2000 · 994 citations · Full text