Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners
Top Cited Papers
Open Access
- 20 March 2008
- journal article
- research article
- Published by Springer Science and Business Media LLC in BMC Genomics
- Vol. 9 (S1), S1
- https://doi.org/10.1186/1471-2164-9-s1-s1
Abstract
Proteins are involved in many interactions with other proteins leading to networks that regulate and control a wide variety of physiological processes. Some of these proteins, called hub proteins or hubs, bind to many different protein partners. Protein intrinsic disorder, via diversity arising from structural plasticity or flexibility, provide a means for hubs to associate with many partners (Dunker AK, Cortese MS, Romero P, Iakoucheva LM, Uversky VN: Flexible Nets: The roles of intrinsic disorder in protein interaction networks. FEBS J 2005, 272:5129-5148). Here we present a detailed examination of two divergent examples: 1) p53, which uses different disordered regions to bind to different partners and which also has several individual disordered regions that each bind to multiple partners, and 2) 14-3-3, which is a structured protein that associates with many different intrinsically disordered partners. For both examples, three-dimensional structures of multiple complexes reveal that the flexibility and plasticity of intrinsically disordered protein regions as well as induced-fit changes in the structured regions are both important for binding diversity. These data support the conjecture that hub proteins often utilize intrinsic disorder to bind to multiple partners and provide detailed information about induced fit in structured regions.Keywords
This publication has 139 references indexed in Scilit:
- Lipid-Binding Activity of Intrinsically Unstructured Cytoplasmic Domains of Multichain Immune Recognition Receptor Signaling SubunitsBiochemistry, 2006
- Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network EvolutionJournal of Proteome Research, 2006
- Abundance of Intrinsic Disorder in Protein Associated with Cardiovascular DiseaseBiochemistry, 2006
- Protein Intrinsic Disorder and Human Papillomaviruses: Increased Amount of Disorder in E6 and E7 Oncoproteins from High Risk HPVsJournal of Proteome Research, 2006
- Intrinsic Disorder in Transcription FactorsBiochemistry, 2006
- Exploiting heterogeneous sequence properties improves prediction of protein disorderProteins, 2005
- Coupled Folding and Binding with α-Helix-Forming Molecular Recognition ElementsBiochemistry, 2005
- Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signalingJournal of Molecular Recognition, 2005
- The iProClass integrated database for protein functional analysisComputational Biology and Chemistry, 2004
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresPeptide Science, 1983