Molecular modeling of the closed forms of the kainate-binding domains of kainate receptors and qualitative analysis of the structure-activity relationships for some agonists

Dokl Biochem Biophys. 2002 Sep-Oct:386:239-44. doi: 10.1023/a:1020799209272.

Authors

M S Belenikin¹, I I Baskin, G Costantino, V A Palyulin, R Pellicciari, N S Zefirov

Affiliation

¹ Department of Chemistry, Moscow State University, Vorob'evy gory, Moscow, 119992 Russia.

PMID: 12469499
DOI: 10.1023/a:1020799209272

No abstract available

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Binding Sites
Binding, Competitive
Kainic Acid / chemistry*
Kainic Acid / metabolism*
Kinetics
Ligands
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Receptors, Kainic Acid / agonists*
Receptors, Kainic Acid / chemistry*
Receptors, Kainic Acid / metabolism
Sequence Alignment
Structure-Activity Relationship
Substrate Specificity

Substances

Ligands
Receptors, Kainic Acid
Kainic Acid