Structure and Features of Amino Acid Sequences of L-Modules in SH3-Like Folds View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-11

AUTHORS

A. M. Kargatov, E. V. Brazhnikov, A. V. Efimov

ABSTRACT

A novel L-shaped repeat module whose structure can be represented as β-strand–loop–β-strand has been identified in a stereochemical analysis of nonhomologous SH3-like folds. β-Strands of the L-module are positioned at a ~90° angle to each other in different orthogonally packed β-layers. Together with a crossover loop, they form a half-turn of a right-handed superhelix. A database of 60 nonhomologous SH3-like domains has been compiled using the Protein Data Bank to study structural similarities and differences of L-modules. Occurrence frequencies of L-modules have been determined depending on the length of their loops. It has been shown that L-modules with βmαααβn- and βmαααβαβn-conformations, where m and n are numbers of β-residues in the first and second β-strands, occur most often (57 and 8%, respectively). Spatial structures of L-modules of the same type are very similar, demonstrated through superimposing them using computer programs. Structural alignment of the amino acid sequences encoding L-modules has been performed, making it possible to identify key positions for hydrophobic, hydrophilic, and proline residues. More... »

PAGES

929-936

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0026893318060092

DOI

http://dx.doi.org/10.1134/s0026893318060092

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1110893840


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