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Exploration of the Dynamic Properties of Protein Complexes Predicted from Spatially Constrained Protein-Protein Interaction Networks

Figure 5

Visual representation of 3-dimensional complex conformations within cluster 1 (A) and cluster 2 (B).

Distributions of Myo5, Las17 and Rvs161/7 show the most striking conformational changes across the two clusters. Green: Myo5, Dark blue: Las17, Red: Rvs161/167Blue-grey: Core+7; composed of the seven core proteins of the Arp2/3 complex and adaptor proteins Sla1/2, Lsb3, End3, Gly1, Sec4 and the expression product of YNR065C. Symmetry breaking within the extended complex suggests branching versus scission complexes. C: Contact frequency is used to quantitatively assess functional domains and spatial relationships amongst components, typically using a resolution of 20 nm. D: Contact frequency demonstrates symmetry breaking of Myo5 and Rvs161/167, and a Myo5 bias in the distribution of Las17.

Figure 5

doi: https://doi.org/10.1371/journal.pcbi.1003654.g005