| + |
NgBR/DHDDS complex | up-regulates 
|
Protein_glycosylation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281490 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32817466 |
The enzyme, cis-prenyltransferase (cis-PTase), composed of two subunits, NgBR and DHDDS, is essential for protein glycosylation reactions in all higher eukaryotes. Here, we report the crystal structure of the human NgBR/DHDDS complex, which represents an atomic resolution structure for any heterodimeric cis-PTase. The crystal structure sheds light on how NgBR stabilizes DHDDS through dimerization, participates in the enzyme's active site through its C-terminal -RXG- motif, and how phospholipids markedly stimulate cis-PTase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DHDDS | form complex 
binding
|
NgBR/DHDDS complex |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281488 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32817466 |
The enzyme, cis-prenyltransferase (cis-PTase), composed of two subunits, NgBR and DHDDS, is essential for protein glycosylation reactions in all higher eukaryotes. Here, we report the crystal structure of the human NgBR/DHDDS complex, which represents an atomic resolution structure for any heterodimeric cis-PTase. The crystal structure sheds light on how NgBR stabilizes DHDDS through dimerization, participates in the enzyme's active site through its C-terminal -RXG- motif, and how phospholipids markedly stimulate cis-PTase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NUS1 | form complex
binding
|
NgBR/DHDDS complex |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281489 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32817466 |
The enzyme, cis-prenyltransferase (cis-PTase), composed of two subunits, NgBR and DHDDS, is essential for protein glycosylation reactions in all higher eukaryotes. Here, we report the crystal structure of the human NgBR/DHDDS complex, which represents an atomic resolution structure for any heterodimeric cis-PTase. The crystal structure sheds light on how NgBR stabilizes DHDDS through dimerization, participates in the enzyme's active site through its C-terminal -RXG- motif, and how phospholipids markedly stimulate cis-PTase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
NgBR/DHDDS complex