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Hub promiscuity in protein-protein interaction networks - PubMed

️Fri Jan 01 2010

Review

Hub promiscuity in protein-protein interaction networks

Ashwini Patil et al. Int J Mol Sci. 2010.

Erratum in

Int J Mol Sci. 2010;11(8):2791

Abstract

Hubs are proteins with a large number of interactions in a protein-protein interaction network. They are the principal agents in the interaction network and affect its function and stability. Their specific recognition of many different protein partners is of great interest from the structural viewpoint. Over the last few years, the structural properties of hubs have been extensively studied. We review the currently known features that are particular to hubs, possibly affecting their binding ability. Specifically, we look at the levels of intrinsic disorder, surface charge and domain distribution in hubs, as compared to non-hubs, along with differences in their functional domains.

Keywords: hubs; interaction networks; promiscuous binding; protein-protein interactions.

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Figures

**Figure 1.**
Partial human protein-protein interaction network showing scale-free topology. Hubs (proteins with 5 or more interactions) and non-hubs are denoted by red and green nodes, respectively. Interactions are shown by the black links between the nodes.

**Figure 2.**
(a) NMR solution structure of Calmodulin showing the relative motion of one Ca²⁺ binding domain (green) with respect to the other using the flexibility of the central disordered region (red) (PDB ID: 1DMO). (b) X-RAY Crystal structure of a small fragment of the N-terminal disordered region of p53 (red) bound to MDM2 (blue) (PDB ID: 1YCQ).

**Figure 3.**
Surface electrostatic potential of Cofilin (obtained from eF-site [54]) (PDB ID: 1QPV). Negative potential is indicated in red, positive potential in blue and hydropathy in yellow.

**Figure 4.**
Ishikawa (Fishbone) diagram representing the characteristics affecting the interaction promiscuity in hub proteins.

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Hub promiscuity in protein-protein interaction networks - PubMed