Abstract
The small beta barrel is a protein structural domain, highly conserved throughout evolution and hence exhibits a broad diversity of functions. Here we undertake a comprehensive review of the structural features of this domain. We begin with what characterizes the structure and the variable nomenclature that has been used to describe it. We then go on to explore the anatomy of the structure and how functional diversity is achieved, including through establishing a variety of multimeric states, which, if misformed, contribute to disease states. We conclude with work following from such a comprehensive structural study.
Copyright
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