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Article (Scientific journals)
Residues crucial for maintaining short paths in network communication mediate signaling in proteins.
del Sol Mesa, Antonio; Fujihashi, Hirotomo; Amoros, Dolors et al.
2006In Molecular Systems Biology, 2, p. 2006.0019
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Keywords :
Allosteric Regulation; Amino Acids; Conserved Sequence; Protein Conformation; Protein Folding; Proteins/chemistry/physiology
Abstract :
[en] Here, we represent protein structures as residue interacting networks, which are assumed to involve a permanent flow of information between amino acids. By removal of nodes from the protein network, we identify fold centrally conserved residues, which are crucial for sustaining the shortest pathways and thus play key roles in long-range interactions. Analysis of seven protein families (myoglobins, G-protein-coupled receptors, the trypsin class of serine proteases, hemoglobins, oligosaccharide phosphorylases, nuclear receptor ligand-binding domains and retroviral proteases) confirms that experimentally many of these residues are important for allosteric communication. The agreement between the centrally conserved residues, which are key in preserving short path lengths, and residues experimentally suggested to mediate signaling further illustrates that topology plays an important role in network communication. Protein folds have evolved under constraints imposed by function. To maintain function, protein structures need to be robust to mutational events. On the other hand, robustness is accompanied by an extreme sensitivity at some crucial sites. Thus, here we propose that centrally conserved residues, whose removal increases the characteristic path length in protein networks, may relate to the system fragility.
Disciplines :
Life sciences: Multidisciplinary, general & others
Author, co-author :
del Sol Mesa, Antonio ;  University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB)
Fujihashi, Hirotomo
Amoros, Dolors
Nussinov, Ruth
Language :
Title :
Residues crucial for maintaining short paths in network communication mediate signaling in proteins.
Publication date :
13 May 2006
Journal title :
Molecular Systems Biology
Publisher :
Wiley-Blackwell, United States
Volume :
Pages :
Peer reviewed :
Peer Reviewed verified by ORBi


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