Results 51 to 60 of about 3,038,180 (280)

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

open access: yesFEBS 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   +5 more
wiley   +1 more source

The Membrane-Proximal Region of C–C Chemokine Receptor Type 5 Participates in the Infection of HIV-1

open access: yesFrontiers in Immunology, 2017
The initial infection and transmission of HIV-1 requires C–C chemokine receptor type 5 (CCR5). Here, we report that the membrane-proximal region (MPR, aa 22–38) of CCR5 participates in the infection of HIV-1.
Ying-Hua Chen   +8 more
doaj   +1 more source

Substantial conformational change mediated by charge-triad residues of the death effector domain in protein-protein interactions. [PDF]

open access: yesPLoS ONE, 2013
Protein conformational changes are commonly associated with the formation of protein complexes. The non-catalytic death effector domains (DEDs) mediate protein-protein interactions in a variety of cellular processes, including apoptosis, proliferation ...
Edward C Twomey   +3 more
doaj   +1 more source

An abiotic, tetrameric, eight-helix bundle

open access: yes, 2023
Four helically folded aromatic oligoamide sequences containing either a chiral monomer based on 2-(2-aminophenoxy)-propionic acid, an N-terminal (1H)-camphanyl group, or both, were synthesized.
MENKE, Friedericke   +10 more
core   +1 more source

Smaller is better: nanobodies meet NMR

open access: yesFEBS 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

Binding of a potent small-molecule inhibitor of six-helix bundle formation requires interactions with both heptad-repeats of the RSV fusion protein [PDF]

open access: yesProceedings of the National Academy of Sciences, 2009
Six-helix bundle (6HB) formation is an essential step for many viruses that rely on a class I fusion protein to enter a target cell and initiate replication. Because the binding modes of small molecule inhibitors of 6HB formation are largely unknown, precisely how they disrupt 6HB formation remains unclear, and structure-based design of improved ...
Roymans, Dirk   +13 more
openaire   +3 more sources

A stapled lipopeptide platform for preventing and treating highly pathogenic viruses of pandemic potential

open access: yesNature Communications
The continued emergence of highly pathogenic viruses, which either thwart immune- and small molecule-based therapies or lack interventions entirely, mandates alternative approaches, particularly for prompt and facile pre- and post-exposure prophylaxis ...
Gregory H. Bird   +11 more
doaj   +1 more source

Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements. [PDF]

open access: yes, 2001
Item does not contain fulltextWe converted the small homodimeric four-helix bundle repressor of primer protein (Rop) into a monomeric four-helix bundle by introduction of connecting loops. Both left- and right-handed four-helix bundles were produced. The
Sander, C.   +11 more
core   +1 more source

Soft motions encoded by the fold and mediated by conserved hinge sites drive V‐ATPase allosteric machinery and autoinhibition

open access: yesFEBS Letters, EarlyView.
Vacuolar H+‐ATPase (V‐ATPase) is a multisubunit rotary proton pump that acidifies intracellular compartments. Using elastic network models, we identified conserved hinge residues that govern its large‐scale functional motions. We show that intrinsically encoded ‘soft modes’ drive critical functional transitions, including rotary catalysis and ...
Diksha Parwana   +3 more
wiley   +1 more source

Conserved Residue Lys574 in the Cavity of HIV-1 Gp41 Coiled-coil Domain Is Critical for Six-helix Bundle Stability and Virus Entry [PDF]

open access: yesJournal of Biological Chemistry, 2007
The fusion-active HIV-1 gp41 core structure is a stable six-helix bundle (6-HB) formed by its N- and C-terminal heptad-repeat sequences (NHR and CHR). A highly conserved, deep hydrophobic cavity on the surface of the N-helical trimer is important for stability of the 6-HB and serves as an ideal target for developing anti-human immunodeficiency virus ...
Yuxian, He   +8 more
openaire   +2 more sources

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