In domain-swapping, two or more identical protein monomers exchange structural elements and fold into dimers or multimers whose units are structurally similar to the original monomer. Domain-swapping is of biotechnological interest because inhibiting domain-swapping can reduce disease-causing fibrillar protein aggregation. To achieve such inhibition, it is important to understand both the energetics that stabilize the domain-swapped structure and the protein dynamics that enable the swapping. Structure-based models (SBMs) encode the folded structure of the protein in their potential energy functions. Domain-swapping has been implicated in the regulation of protein function. Additionally, domain swapping has been suggested as a mechanism for the evolution of larger complex folds when it is followed by gene duplication and fusion. Open-ended domain-swapping can lead to the formation of large protein aggregates. In some conditions, aggregation can lead to the loss of protein function and cause disease. Here you have an amazing recent example of a domain swapped protein dimer, represented by the crystal structure of a putative ribonuclease from Mycobacterium tuberculosis (PDB code: 8H0H)

#molecularart ... #immolecular ... #domainswapping ... #dimer ... #catalysis ... #xray ... #mycobacterium

Structure rendered with @proteinimaging and depicted with @corelphotopaint