Modeling Ion Selectivity in Transmembrane Domain of the NMDA Receptor
نویسندگان
چکیده
منابع مشابه
The transmembrane domain of the 5-HT3 receptor: its role in selectivity and gating.
The 5-HT3 (5-hydroxytryptamine) receptor is a typical member of the Cys-loop family of ligand-gated ion channels. No atomic resolution structures of these proteins have yet been published, and thus structure-function relationships in this family of proteins have been largely determined from experimental evidence combined with the use of homologous proteins and lower resolution images. Here, rec...
متن کاملA novel NMDA receptor positive allosteric modulator that acts via the transmembrane domain
Ionotropic glutamate receptors (iGluRs) mediate fast excitatory neurotransmission and are key nervous system drug targets. While diverse pharmacological tools have yielded insight into iGluR extracellular domain function, less is known about molecular mechanisms underlying the ion conduction gating process within the transmembrane domain (TMD). We have discovered a novel NMDAR positive alloster...
متن کاملAll atom NMDA receptor transmembrane domain model development and simulations in lipid bilayers and water
N-methyl-d-aspartate receptors (NMDARs) are members of the ionotropic glutamate receptor family that mediate excitatory synaptic transmission in the central nervous system. The channels of NMDARs are permeable to Ca2+ but blocked by Mg2+, distinctive properties that underlie essential brain processes such as induction of synaptic plasticity. However, due to limited structural information about ...
متن کاملNicotinic Receptor Fourth Transmembrane Domain
The fourth transmembrane domain (M4) of the nicotinic acetylcholine receptor (AChR) contributes to the kinetics of activation, yet its close association with the lipid bilayer makes it the outermost of the transmembrane domains. To investigate mechanistic and structural contributions of M4 to AChR activation, we systematically mutated alphaT422, a conserved residue that has been labeled by hydr...
متن کاملConverting a transmembrane receptor to a soluble receptor: recognition domain to effector domain signaling after excision of the transmembrane domain.
The bacterial aspartate receptor was reconstructed to eliminate the transmembrane domain, thus connecting the recognition domain directly to the effector domain. The resulting soluble receptor folded correctly and was no longer an integral membrane protein. Upon aspartate binding, this soluble receptor was stabilized to a similar extent as that of the native receptor. Of interest, this soluble ...
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: Biophysical Journal
سال: 2017
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2016.11.2262