Nov 8, 2018

Pseudo-Symmetry and Conformational Plasticity in 7 Transmembrane Helix (7TMH) Proteins: Intragenic Duplication and Assembly of 3TMH or 4TMH Protodomains with Evolutionary Balance of Structural Constraints and Functional Divergence

BioRxiv : the Preprint Server for Biology
Philippe YoukharibacheRavi Abrol

Abstract

7-Transmembrane-Helix (7TMH) proteins cannot be grouped under a monolithic fold or superfold. A parallel structure-based analysis of pseudo-symmetric membrane domains around that magic number of 7 transmembrane helices, reveals a possible intragenic duplication pattern in their construction. A number of distinct 6/7/8-TMH proteins are examined: MFS, SWEET, PnuC, TRIC, FocA, Aquaporin, and GPCRs, which show evidence of a duplication pattern of a 3 or 4 Transmembrane Helix (3/4-TMH) protodomain, the unifying theme in all membrane proteins examined in this study. Our analysis leads to guiding principles of protodomain assembly and to envision the role of conformational plasticity in fold formation and functional divergence. It also provides a structural and mechanistic framework for the evolutionary deconstruction and reconstruction of current pseudo-symmetrical transmembrane helical (TMH) proteins. In particular, the transmembrane (TM) sequences of intracellular and extracellular facing halves reflect the co-evolution of these protodomains within 6/7/8-TMH pseudo-symmetric domains under functional and structural constraints, especially in the case of G protein coupled receptors (GPCRs). The sequence/structure analysis of differen...Continue Reading

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Mentioned in this Paper

Study
Molecular Helix
Extracellular
Membrane
Symmetrical Synapse
G-Protein-Coupled Receptors
Integral Membrane Proteins
Reconstructive Surgical Procedures
Transmembrane Domain
Protoplasm

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