Motifs involved in protein-protein interactions

Autor:	O. A. Bateman, A. Simpson, Christine Slingsby
Rok vydání:	1993
Předmět:	Models Molecular Helix bundle Protein Conformation Chemistry Stereochemistry Beta sheet Rotational symmetry Proteins General Medicine Oligomer Protein–protein interaction chemistry.chemical_compound Monomer Biochemistry Genetics Molecular Biology Structural unit Protein secondary structure
Zdroj:	Molecular Biology Reports. 17:185-195
ISSN:	1573-4978 0301-4851
DOI:	10.1007/bf00986727
Popis:	Interactions between proteins are extremely variable. However, in the dimeric proteins comprised of regular motifs, interface interactions are similar to those that stabilize monomers. Additional stability is gained by converting loops within motifs or domains to linkers across interfaces. In multi-domain proteins, interactions can be greatly effected by the conformation of linkers between domains. Complex association of subunits, involving higher rotational symmetry or cubic symmetry, frequently involves motif sharing across interfaces.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cea1368d55b1d30e03a27fee3042e57 https://doi.org/10.1007/bf00986727 Zobrazit plný text záznamu Full text from SpringerLink