+ |
PRIM2 | form complex
binding
|
DNA primase complex |
0.99 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261340 |
|
|
in vitro |
|
pmid |
sentence |
24043831 |
Here, we describe the crystal structure of human primase in heterodimeric form consisting of full-length catalytic subunit and a C-terminally truncated large subunit. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PRIM1 | form complex
binding
|
DNA primase complex |
0.99 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261339 |
|
|
in vitro |
|
pmid |
sentence |
24043831 |
Here, we describe the crystal structure of human primase in heterodimeric form consisting of full-length catalytic subunit and a C-terminally truncated large subunit. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
DNA primase complex | form complex
binding
|
DNA polymerase alpha:primase complex |
0.986 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261341 |
|
|
in vitro |
|
pmid |
sentence |
24043831 |
At the replication fork, primase is present in a constitutive complex with DNA polymerase α (Pol α), which extends the RNA primer with deoxynucleotides and makes the resulting RNA–DNA primer available to the leading- and lagging-strand polymerases, Pols ε and δ, for processive elongation |
|
Publications: |
1 |
Organism: |
In Vitro |