PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 6261141

Membrane protein oligomeric structure and transport function.

M Klingenberg
View original source ↗Export metadata ↓

Abstract

Proteins which traverse membranes tend to have a dimeric structure in which the dimer is arranged asymmetrically across the membrane with the axis of symmetry perpendicular to the membrane plane. This general structure is well suited to the function of transporting nutrients across the cell membrane.

Explore related subjects

Carrier ProteinsCell MembraneIon ChannelsMacromolecular SubstancesMembrane LipidsMembrane ProteinsPhospholipidsProtein ConformationSodium-Potassium-Exchanging ATPaseStructure-Activity RelationshipJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M Klingenberg. 1981-04-09. Membrane protein oligomeric structure and transport function.. https://doi.org/10.1038/290449a0

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Electrochemical screening of recombinant protein solubility in Escherichia coli using scanning electrochemical microscopy (SECM).

A microbial array chip with collagen gel spots entrapping living Escherichia coli (E. coli) DH5alpha was applied for the screening of recombinant protein solubilities. The alpha-fragment of beta-galactosidase (betaGal) was fused to the target protein, namely, maltose-binding protein (MBP), to monitor the solubility of MBP. Scanning electrochemical microscopy (SECM) was used to detect the release of p-aminophenol from E. coli cells catalyzed by intracellular betaGal. Comparison of the SECM-based method with the Western blotting-based method indicated that the current response obtained using SECM increased with an increase in the betaGal activity and therefore, with the soluble fraction of MBP in the host cells.

Carrier Proteins↗
PubMed2007

Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.

Although cullin-1 neddylation is crucial for the activation of SCF ubiquitin E3 ligases, the underlying mechanisms for NEDD8-mediated activation of SCF remain unclear. Here we demonstrate by NMR and mutational studies that NEDD8 binds the ubiquitin E2 (UBC4), but not NEDD8 E2 (UBC12). Our data imply that NEDD8 forms an active platform on the SCF complex for selective recruitment of ubiquitin-charged E2s in collaboration with RBX1, and thereby upregulates the E3 activity.

Carrier Proteins↗