Abstract
A new method for studying signal transmission between functional sites by decomposing protein structures into modules demonstrates that protein domains consist of modules interconnected by residues that mediate signaling through the shortest pathways.
Highlights
Allosteric communications are vital for cellular signaling
Comparison of contacts between amino acids belonging to different modules and those between amino acids belonging to the same module revealed that the percentage of long-range interactions is larger in the inter-modular contacts (Figure 2)
Experimental studies confirm that interdomain linker regions are crucial for the domain coupling required for the information transfer [16]
Summary
Allosteric communications are vital for cellular signaling. Here we explore a relationship between protein architectural organization and shortcuts in signaling pathways. The role of the pre-existing equilibrium of conformational sub-states in allostery proposed already over 20 years ago [6] is increasingly receiving attention, emphasizing the key role of protein dynamics in this process [1,7,8,9] Experimental methods such as double mutant cycle analysis [10] have provided insights into allosteric communications, understanding the general principles of the transmission of information between distant functional surfaces remains a challenge in structural biology. The model allows us to determine fold centrally conserved residues (FCCRs) These residues are responsible for maintaining the shortest pathways between all amino acids and, play key roles in signal transmission [13]. Perceiving protein structures as information processing networks, it is reasonable to assume that mutations of amino acids crucial for network communications could impair signal transmission
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