Thermodynamic modeling reveals widespread multivalent binding by RNA-binding proteins
Author(s) -
Salma Sohrabi-Jahromi,
Johannes Söding
Publication year - 2021
Publication title -
bioinformatics
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btab300
Subject(s) - rna , rna binding protein , computational biology , binding site , binding selectivity , plasma protein binding , riboswitch , biology , sequence motif , bipartite graph , genetics , microbiology and biotechnology , computer science , dna , non coding rna , biochemistry , theoretical computer science , gene , graph
Understanding how proteins recognize their RNA targets is essential to elucidate regulatory processes in the cell. Many RNA-binding proteins (RBPs) form complexes or have multiple domains that allow them to bind to RNA in a multivalent, cooperative manner. They can thereby achieve higher specificity and affinity than proteins with a single RNA-binding domain. However, current approaches to de novo discovery of RNA binding motifs do not take multivalent binding into account.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom