Assessing Protein Function Through Structural Similarities with CATH

Natalie L Dawson; Christine Orengo; Zoltán Gáspári

doi:10.1007/978-1-0716-0270-6_4

Assessing Protein Function Through Structural Similarities with CATH

Methods Mol Biol. 2020:2112:43-57. doi: 10.1007/978-1-0716-0270-6_4.

Authors

Natalie L Dawson¹, Christine Orengo², Zoltán Gáspári³

Affiliations

¹ Institute of Structural and Molecular Biology, University College London, London, UK. natalie.dawson.09@ucl.ac.uk.
² Institute of Structural and Molecular Biology, University College London, London, UK.
³ Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.

PMID: 32006277
DOI: 10.1007/978-1-0716-0270-6_4

Abstract

The functional diversity of proteins is closely related to their differences in sequence and structure. Despite variations in functional sites, global structural similarity is a valuable source of information when assessing potential functional similarities between proteins. The CATH database contains a well-established hierarchical classification of more than 430,000 protein domain structures and nearly 95 million protein domain sequences, with integrated functional annotations for each represented family. The present chapter provides an overview of the main features of CATH with emphasis on exploiting structural similarities to obtain functional information for proteins.

Keywords: Functional assignment; Protein function; Protein structure; Structure classification; Structure similarity.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Databases, Protein
Protein Structure, Tertiary
Proteins / chemistry*
Sequence Analysis, Protein*
Sequence Homology, Amino Acid*
Structural Homology, Protein*

Substances

Proteins

Grants and funding

104960/Z/14/Z/WT_/Wellcome Trust/United Kingdom