Druggability Simulations and X-Ray Crystallography Reveal a Ligand-Binding Site in the GluA3 AMPA Receptor N-Terminal Domain
نویسندگان
چکیده
منابع مشابه
AMPA receptor ligand-binding domain: Site-directed mutagenesis study of ligand-receptor interactions
Academic Dissertation To be presented for public criticism, with the permission of the Faculty of Science of the (1998) Disulfide bonding and cysteine accessibility in the α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluRD. Implications for redox modulation of glutamate receptors. receptors and bacterial periplasmic amino acid-binding proteins share the ionic mechanism ...
متن کاملThe X-ray Transform and its Application in Nano Crystallography
In this article a review on the definition of the X- ray transform and some ofits applications in Nano crystallography is presented. We shall show that the X- raytransform is a special case of the Radon transform on homogeneous spaces when thetopological group E(n)- the Euclidean group - acts on ℝ2 transitively. First someproperties of the Radon transform are investigated then the relationship ...
متن کاملStargazin promotes closure of the AMPA receptor ligand-binding domain
Transmembrane AMPA receptor (AMPAR) regulatory proteins (TARPs) markedly enhance AMPAR function, altering ligand efficacy and receptor gating kinetics and thereby shaping the postsynaptic response. The structural mechanism underlying TARP effects on gating, however, is unknown. Here we find that the prototypical member of the TARP family, stargazin or γ-2, rescues gating deficits in AMPARs carr...
متن کاملUnique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations
The 16 EphA and EphB receptors represent the largest family of receptor tyrosine kinases, and their interactions with 9 ephrin-A and ephrin-B ligands initiate bidirectional signals controlling many physiological and pathological processes. Most interactions occur between receptor and ephrins of the same class, and only EphA4 can bind all A and B ephrins. To understand the structural and dynamic...
متن کاملThe N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling.
The Eph family of receptor protein-tyrosine kinases (RTKs) have recently been implicated in patterning and wiring events in the developing nervous system. Eph receptors are unique among other RTKs in that they fall into two large subclasses that show distinct ligand specificities and for the fact that they themselves might function as 'ligands', thereby activating bidirectional signaling. To ga...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Structure
سال: 2019
ISSN: 0969-2126
DOI: 10.1016/j.str.2018.10.017