| + |
CAPZA2 | form complex 
binding
|
F-actin capping protein complex, CAPZA2 variant |
0.954 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281369 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 37228182 |
CapZ is a heterodimer of related α and β subunits (Fig. 2A) (12). The heterodimer is described as having a mushroom-like shape, where the mushroom head binds the barbed end (Fig. 2B). The barbed and pointed ends of the actin filament (F-actin) are the sites of growth/shrinkage and the targets of capping proteins that block subunit exchange, including CapZ at the barbed end and tropomodulin at the pointed end. We describe cryo-EM structures of the free and capped ends of F-actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
F-actin capping protein complex, CAPZA2 variant | up-regulates 
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281368 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 37228182 |
CapZ is a heterodimer of related α and β subunits (Fig. 2A) (12). The heterodimer is described as having a mushroom-like shape, where the mushroom head binds the barbed end (Fig. 2B). The barbed and pointed ends of the actin filament (F-actin) are the sites of growth/shrinkage and the targets of capping proteins that block subunit exchange, including CapZ at the barbed end and tropomodulin at the pointed end. We describe cryo-EM structures of the free and capped ends of F-actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAPZB | form complex
binding
|
F-actin capping protein complex, CAPZA2 variant |
0.954 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281370 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 37228182 |
CapZ is a heterodimer of related α and β subunits (Fig. 2A) (12). The heterodimer is described as having a mushroom-like shape, where the mushroom head binds the barbed end (Fig. 2B). The barbed and pointed ends of the actin filament (F-actin) are the sites of growth/shrinkage and the targets of capping proteins that block subunit exchange, including CapZ at the barbed end and tropomodulin at the pointed end. We describe cryo-EM structures of the free and capped ends of F-actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
F-actin capping protein complex, CAPZA2 variant