Crystal Structure of GluR2 ligand binding core in complex with Quisqualate

Crystal Structure of GluR2 ligand binding core in complex with Quisqualate 1MM6

Glutamate receptor 2 is a protein encoded by the GRIA2 gene. It is the major excitatory neurotransmitter in the mammalian brain as it mediates most of the fast excitatory synaptic transmission in the mammalian central nervous system.

Quisqualate is a high-affinity receptor that elicits maximum peak current responses, and stabilizes the ligand binding core in a fully closed conformation In red are the QUS receptor sites.

The mechanism of quisqualate binding is different from that of AMPA but similar to that of glutamate • A comparison of the three complexes reveals distinct binding mechanisms, particularly in the region of a hydrophobic pocket • The hydrophobic pocket, plays an important role in determining receptor subtype specificity. The regions in blue are hydrophobic

Crystal Structure of GluR2 ligand binding core in complex with Quisqualate

Crystal Structure of GluR2 ligand binding core in complex with Quisqualate

Presentation Transcript

Crystal structure of Diamond

II. Crystal Structure

Ligand configurational entropy and protein binding

CRYSTAL STRUCTURE

Computational Design of Ligand-binding Proteins with High Affinity and Selectivity

Crystal Honeycomb Structure of Ice

CRYSTAL STRUCTURE

Crystal Structure

§2.4 Crystal Structure and Complex Lattice

Crystal structure

General Properties of Complex Binding Function - Structure Relationships

Predicting ligand binding sites on protein surface

Crystal Structure Validation with PLATON

RUTILE CRYSTAL STRUCTURE

Crystal Structure

CRYSTAL STRUCTURE

Crystal Structure Continued!

Crystal Structure

1. Crystal Structure

Crystal structure of Diamond

Crystal Structure