Abstract
The Structural Classification of Proteins (SCOP) database has facilitated the development of many tools and algorithms and it has been successfully used in protein structure prediction and large-scale genome annotations. During the development of SCOP, numerous exceptions were found to topological rules, along with complex evolutionary scenarios and peculiarities in proteins including the ability to fold into alternative structures. This article reviews cases of structural variations observed for individual proteins and among groups of homologues, knowledge of which is essential for protein structure modelling.
Highlights
Over the past two decades, the Structural Classification of Proteins (SCOP) database has become an essential resource in many areas of protein research [1]
Designed to assist structural biologists in the analysis of structural similarities between proteins, SCOP facilitated the development of tools and algorithms and it has been successfully used in protein structure prediction and large-scale genome annotations [2,3]
SCOP contributed to our understanding of protein repertoire, including how proteins relate to each other and how their structures and functions evolved [4]
Summary
Over the past two decades, the Structural Classification of Proteins (SCOP) database has become an essential resource in many areas of protein research [1]. The classification of proteins in SCOP depends on their relationships to proteins with known 3D structure and their identification typically includes a sequence similarity search against a database Undergo much larger structural rearrangements, leading to a conformational transition from one stable folded state to another.
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