NDLI: Light on the structural communication in Ras GTPases.

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Light on the structural communication in Ras GTPases.

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Light on the structural communication in Ras GTPases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Raimondi, Francesco Felline, Angelo Portella, Guillem Orozco, Modesto Fanelli, Francesca
Description	Country affiliation: Italy Author Affiliation: Raimondi F ( Department of Chemistry, University of Modena and Reggio Emilia, Modena, Italy.)
Abstract	The graph theory was combined with fluctuation dynamics to investigate the structural communication in four small G proteins, Arf1, H-Ras, RhoA, and Sec4. The topology of small GTPases is such that it requires the presence of the nucleotide to acquire a persistent structural network. The majority of communication paths involves the nucleotide and does not exist in the unbound forms. The latter are almost devoid of high-frequency paths. Thus, small Ras GTPases acquire the ability to transfer signals in the presence of nucleotide, suggesting that it modifies the intrinsic dynamics of the protein through the establishment of regions of hyperlinked nodes with high occurrence of correlated motions. The analysis of communication paths in the inactive (S(GDP)) and active (S(GTP)) states of the four G proteins strengthened the separation of the Ras-like domain into two dynamically distinct lobes, i.e. lobes 1 and 2, representing, respectively, the N-terminal and C-terminal halves of the domain. In the framework of this separation, interfunctional states and interfamily differences could be inferred. The structure network undergoes a reshaping depending on the bound nucleotide. Nucleotide-dependent divergences in structural communication reach the maximum in Arf1 and the minimum in RhoA. In Arf1, the nucleotide-dependent paths essentially express a communication between the G box 4 (G4) and distal portions of lobe 1. In the S(GDP) state, the G4 communicates with the N-term, while, in the S(GTP) state, the G4 communicates with the switch II. Clear differences could be also found between Arf1 and the other three G proteins. In Arf1, the nucleotide tends to communicate with distal portions of lobe 1, whereas in H-Ras, RhoA, and Sec4 it tends to communicate with a cluster of aromatic/hydrophobic amino acids in lobe 2. These differences may be linked, at least in part, to the divergent membrane anchoring modes that would involve the N-term for the Arf family and the C-term for the Rab/Ras/Rho families.
File Format	HTM / HTML
ISSN	07391102
Issue Number	2
Volume Number	31
e-ISSN	15380254
Journal	Journal of Biomolecular Structure and Dynamics
Language	English
Publisher	Taylor & Francis
Publisher Date	2013-01-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Discipline Biochemistry Adp-ribosylation Factor 1 Chemistry Molecular Dynamics Simulation Proto-oncogene Proteins P21(ras) Saccharomyces Cerevisiae Proteins Rab Gtp-binding Proteins Rhoa Gtp-binding Protein Amino Acid Sequence Guanine Nucleotides Humans Magnesium Molecular Sequence Data Protein Binding Protein Structure, Secondary Saccharomyces Cerevisiae Structural Homology, Protein Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Medicine Molecular Biology

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