Pub. Date : 1999 Jan 1
PMID : 9867876
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4. | Cysteine | discs large MAGUK scaffold protein 4 | Homo sapiens |
2 | Requirement of N-terminal cysteines of PSD-95 for PSD-95 multimerization and ternary complex formation, but not for binding to potassium channel Kv1.4. | Cysteine | discs large MAGUK scaffold protein 4 | Homo sapiens |
3 | A pair of N-terminal cysteines, Cys3 and Cys5, is essential for the ability of PSD-95 to self-associate and to form cell surface clusters with Kv1.4. | Cysteine | discs large MAGUK scaffold protein 4 | Homo sapiens |
4 | However, PSD-95 mutants lacking these cysteine residues retain their ability to associate with membranes and to bind to Kv1.4. | Cysteine | discs large MAGUK scaffold protein 4 | Homo sapiens |
5 | Unlike wild type PSD-95, the cysteine mutant of PSD-95 cannot form a ternary complex with Kv1.4 and the cell adhesion molecule Fasciclin II. | Cysteine | discs large MAGUK scaffold protein 4 | Homo sapiens |
6 | These results suggest that the N-terminal cysteines are essential for PSD-95 multimerization and that multimerization is required for simultaneous binding of multiple membrane protein ligands by PSD-95. | Cysteine | discs large MAGUK scaffold protein 4 | Homo sapiens |