Many-to-one binding by intrinsically disordered protein regions

Wei Lun Alterovitz, Eshel Faraggi, Christopher J. Oldfield, Jingwei Meng, Bin Xue, Fei Huang, Pedro Romero, Andrzej Kloczkowski, Vladimir N. Uversky, A. Keith Dunker

Research output: Contribution to journalArticle

Abstract

Disordered binding regions (DBRs), which are embedded within intrinsically disordered proteins or regions (IDPs or IDRs), enable IDPs or IDRs to mediate multiple protein-protein interactions. DBR-protein complexes were collected from the Protein Data Bank for which two or more DBRs having different amino acid sequences bind to the same (100% sequence identical) globular protein partner, a type of interaction herein called many-to-one binding. Two distinct binding profiles were identified: independent and overlapping. For the overlapping binding profiles, the distinct DBRs interact by means of almost identical binding sites (herein called "similar"), or the binding sites contain both common and divergent interaction residues (herein called "intersecting"). Further analysis of the sequence and structural differences among these three groups indicate how IDP flexibility allows different segments to adjust to similar, intersecting, and independent binding pockets.

Original languageEnglish (US)
Pages (from-to)159-170
Number of pages12
JournalPacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
Volume25
StatePublished - Jan 1 2020

ASJC Scopus subject areas

  • Biomedical Engineering
  • Computational Theory and Mathematics

Fingerprint Dive into the research topics of 'Many-to-one binding by intrinsically disordered protein regions'. Together they form a unique fingerprint.

  • Cite this

    Alterovitz, W. L., Faraggi, E., Oldfield, C. J., Meng, J., Xue, B., Huang, F., Romero, P., Kloczkowski, A., Uversky, V. N., & Dunker, A. K. (2020). Many-to-one binding by intrinsically disordered protein regions. Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing, 25, 159-170.