Reference : Topology of small-world networks of protein-protein complex structures.
Scientific journals : Article
Life sciences : Multidisciplinary, general & others
http://hdl.handle.net/10993/17849
Topology of small-world networks of protein-protein complex structures.
English
del Sol Mesa, Antonio mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) >]
Fujihashi, Hirotomo [> >]
O'Meara, Paul [> >]
2005
Bioinformatics (Oxford, England)
21
8
1311-5
Yes (verified by ORBilu)
1367-4803
England
[en] Binding Sites ; Computer Simulation ; Dimerization ; Models, Biological ; Models, Chemical ; Multiprotein Complexes/chemistry/metabolism ; Protein Binding ; Protein Interaction Mapping/methods ; Proteins/chemistry/metabolism ; Sequence Analysis, Protein/methods ; Signal Transduction/physiology ; Structure-Activity Relationship
[en] The majority of real examples of small-world networks exhibit a power law distribution of edges among the nodes, therefore not fitting into the wiring model proposed by Watts and Strogatz. However, protein structures can be modeled as small-world networks, with a distribution of the number of links decaying exponentially as in the case of this wiring model. We approach the protein-protein interaction mechanism by viewing it as a particular rewiring occurring in the system of two small-world networks represented by the monomers, where a re-arrangement of links takes place upon dimerization leaving the small-world character in the dimer network. Due to this rewiring, the most central residues at the complex interfaces tend to form clusters, which are not homogenously distributed. We show that these highly central residues are strongly correlated with the presence of hot spots of binding free energy. CONTACT: ao-mesa@fujirebio.co.jp SUPPLEMENTARY INFORMATION: http://www.fujirebio.co.jp/support/index.php (under construction).
http://hdl.handle.net/10993/17849

There is no file associated with this reference.

Bookmark and Share SFX Query

All documents in ORBilu are protected by a user license.