Results 41 to 50 of about 434,631 (260)

HIV and the 7-Transmembrane Domain Receptors

Pathobiology, 2008
The recent discovery of a chemokine receptor, fusin (fusin/CXCR-4), as the long-sought human immunodeficiency virus type 1 (HIV-1) coreceptor opened an entirely new field of aquired immunodeficiency syndrome (AIDS) research on mechanisms of viral entry, tropism and pathogenesis. It was soon followed by the identification of the chemokine receptor CCR-5
Broder, Christopher C., Dimitrov, Dimiter S.   +1 more
openaire   +2 more sources

Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions

FEBS Letters, EarlyView.
The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang, Hyo Been Jin, Chang Min Kim, So Yeon Lee, Hyun Ho Park   +4 more
wiley   +1 more source

Animal septins contain functional transmembrane domains

Current Biology, 2023
Summary Septins, a conserved family of filament-forming proteins, contribute to eukaryotic cell division, polarity, and membrane trafficking. Septins scaffold other proteins to cellular membranes, but it is not fully understood how septins associate with membranes. We identified and characterized an isoform of
Perry, Jenna, Werner, Michael, Omi, Shizue, Heck, Bryan, Maddox, Paul, Mavrakis, Manos, Maddox, Amy Shaub   +6 more
openaire   +4 more sources

Structure‐forward targeting of claudins with synthetic binders

FEBS Letters, EarlyView.
Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley   +1 more source

Domain-domain associations in cystic fibrosis transmembrane conductance regulator [PDF]

American Journal of Physiology-Cell Physiology, 2002
Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. CFTR is a chloride channel whose activity requires protein kinase A-dependent phosphorylation of an intracellular regulatory domain (R-domain) and ATP hydrolysis at the nucleotide-binding domains (NBDs).
Wenlan, Wang, Zhaoping, He, Thomas J, O'Shaughnessy, John, Rux, William W, Reenstra   +4 more
openaire   +2 more sources

The role of prolines and glycine in the transmembrane domain of LAT [PDF]

The FEBS Journal, 2020
ABSTRACT LAT is a critical regulator of T cell development and function. It organises signalling events at the plasma membrane. However, the mechanism, which controls LAT localisation at the plasma membrane is not fully understood. Here, we studied the impact of helix-breaking amino acids, two prolines and one glycine,
Daniela Glatzová, Harsha Mavila, Maria Chiara Saija, Tomáš Chum, Lukasz Cwiklik, Tomáš Brdička, Marek Cebecauer   +6 more
openaire   +3 more sources

The heterodimeric amino acid transporters (HAT) of the SLC7/SLC3 family: A structure−function relationships and relevance to human pathology

FEBS Letters, EarlyView.
Heterodimeric amino acid transporters consist of SLC7 and SLC3 family proteins arranged in a conserved structural organization. They regulate nutrient transport across cell membranes, supporting essential cellular functions. These transporters also contribute to xenobiotic/drug uptake and distribution.
Mariafrancesca Scalise, Tiziano Mazza, Raffaella Scanga, Lara Console, Michele Galluccio, Cesare Indiveri   +5 more
wiley   +1 more source

A Transmembrane Domain GGxxG Motif in CD4 Contributes to Its Lck-Independent Function but Does Not Mediate CD4 Dimerization. [PDF]

PLoS ONE, 2015
CD4 interactions with class II major histocompatibility complex (MHC) molecules are essential for CD4+ T cell development, activation, and effector functions.
Heather L Parrish, Caleb R Glassman, Madeline M Keenen, Neha R Deshpande, Matthew P Bronnimann, Michael S Kuhns   +5 more
doaj   +1 more source

Leucine‐rich glioma inactivated 1 (LGI1) is a ganglioside‐binding protein

FEBS Letters, EarlyView.
Neuronal hyperexcitability associated with a decrease/absence of the extracellular protein LGI1 has been suggested to be primarily due to the downregulation of Kv1 channel expression. The molecular mechanisms underlying this decrease have not yet been elucidated.
Kévin Debreux, Christian Lévêque, Fodil Azzaz, Marion Sangiardi, Sarosh R Irani, Michael Seagar, Jacques Fantini, Oussama El Far   +7 more
wiley   +1 more source

Smaller is better: nanobodies meet NMR

FEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source