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ABSTRACT: Background
Large surface loops contained within compact protein structures and not involved in catalytic process have been proposed as preferred regions for protein family evolution. These loops are subjected to lower sequence constraints and can evolve rapidly in novel structural variants. A good model to study this hypothesis is represented by sialidase enzymes. Indeed, the structure of sialidases is a β-propeller composed by anti-parallel β-sheets connected by loops that suit well with the rapid evolving loop hypothesis. These features prompted us to extend our studies on this protein family in birds, to get insights on the evolution of this class of glycohydrolases.Results
Gallus gallus (Gg) genome contains one NEU3 gene encoding a protein with a unique 188 amino acid s
SUBMITTER: Giacopuzzi E
PROVIDER: S-EPMC3179935 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature