Multiple Partner, Root Mean Square Fluctuation, Intrinsic Disorder, Bovine Immunodeficiency Virus, Side Chain Conformation
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Background: 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).
Results: 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.
Conclusions: 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.
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Citation / Publisher Attribution
BMC Genomics, v. 9, issue 1, art. S1
This is an Open Access article is distributed under the terms of the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/2.0 ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Scholar Commons Citation
Oldfield, Christopher J.; Meng, Jingwei; Yang, Jack Y.; Yang, Mary Qu; Uversky, Vladimir N.; and Dunker, A. Keith, "Flexible Nets: Disorder and Induced Fit in The Associations of P53 and 14-3-3 with Their Partners" (2008). Molecular Medicine Faculty Publications. 575.