Evidence for the preferential reuse of sub‐domain motifs in primordial protein folds

URN to cite this document:: urn:nbn:de:bvb:355-epub-458125
DOI to cite this document:: 10.5283/epub.45812

Heizinger, Leonhard ; Merkl, Rainer

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Date of publication of this fulltext: 19 May 2021 05:43

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Abstract

A comparison of protein backbones makes clear that not more than approximately 1400 different folds exist, each specifying the three-dimensional topology of a protein domain. Large proteins are composed of specific domain combinations and many domains can accommodate different functions. These findings confirm that the reuse of domains is key for the evolution of multi-domain proteins. If reuse ...