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Journal Article
Membrane-protein topology
2006
Overview
Key Points
The topology of an integral membrane protein describes the number and approximate locations in the sequence of the transmembrane segments, as well as the overall orientation of the protein in a membrane.
Topology is controlled primarily by the hydrophobicity and length of transmembrane helices as well as the distribution of positively charged residues in the loops that connect the helices.
In most cases, topology is determined co-translationally during the translocon-mediated insertion of a polypeptide into a membrane.
Topologies in which both the N terminus and the C terminus of a protein are in the cytoplasm are predominant in both prokaryotic and eukaryotic cells.
Membrane proteins evolve primarily by gene duplication and gene fusion. Many membrane proteins form dimers in which the two homologous chains have the same topology (parallel dimer) or opposite topologies (antiparallel dimer). Gene fusions create internally duplicated structures in which the two halves of a protein are orientated either in a parallel or an antiparallel manner.
The concept of membrane-protein topology is at least 30-years old. However, proteome-wide data on topology, increasing numbers of high-resolution structures and detailed studies on individual proteins are now showing us how topology is determined by the amino-acid sequence.
In the world of membrane proteins, topology defines an important halfway house between the amino-acid sequence and the fully folded three-dimensional structure. Although the concept of membrane-protein topology dates back at least 30 years, recent advances in the field of translocon-mediated membrane-protein assembly, proteome-wide studies of membrane-protein topology and an exponentially growing number of high-resolution membrane-protein structures have given us a deeper understanding of how topology is determined and of how it evolves.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Biomedical and Life Sciences
/ Humans
/ Hydrophobic and Hydrophilic Interactions
/ Intracellular Membranes - chemistry
/ Membrane Proteins - chemistry
/ Membrane Proteins - genetics
/ Membrane Proteins - metabolism
/ Membrane Proteins/chemistry/genetics/metabolism
/ Proteins
/ Proteome
/ Protons
/ Topology
