Replication protein E1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
- | The complex between BPV1 DBD and 21-bp DNA (PDB code [[1ksx]]) shows 2 DBD-DNA binding modules: a binding loop and a binding helix each interacting with a single strand. The protein-DNA interactions are hydrophilic to phosphate atoms and van der Waals hydrophobic ones<ref>PMID:11889054</ref>. | + | The complex between BPV1 DBD and 21-bp DNA (PDB code [[1ksx]]) shows 2 DBD-DNA binding modules: a <scene name='87/873777/Cv/2'>binding loop</scene> and a <scene name='87/873777/Cv/4'>binding helix</scene> each interacting with a single strand. The protein-DNA interactions are hydrophilic to phosphate atoms and van der Waals hydrophobic ones<ref>PMID:11889054</ref>. |
</StructureSection> | </StructureSection> | ||
==3D structures of replication protein E1== | ==3D structures of replication protein E1== |
Revision as of 12:38, 3 February 2021
|
3D structures of replication protein E1
Updated on 03-February-2021
Domains: helicase 301-605; DNA-binding (DBD) 286-365
1r9w - RPE1 DBD - HPV18
1tue - RPE1 428-631 (mutant) + RPE2 TAD
2v9p - RPE1 helicase domain - BPV1
5a9k - RPE1 helicase domain - Cryo EM
2gxa - RPE1 helicase domain + DNA + ADP
1f08 - RPE1 DBD
1ksx, 1ksy - RPE1 DBD + DNA
References
- ↑ Wilson VG, West M, Woytek K, Rangasamy D. Papillomavirus E1 proteins: form, function, and features. Virus Genes. 2002 Jun;24(3):275-90. doi: 10.1023/a:1015336817836. PMID:12086149 doi:http://dx.doi.org/10.1023/a:1015336817836
- ↑ Baedyananda F, Chaiwongkot A, Bhattarakosol P. Elevated HPV16 E1 Expression Is Associated with Cervical Cancer Progression. Intervirology. 2017;60(5):171-180. doi: 10.1159/000487048. Epub 2018 Mar 1. PMID:29495005 doi:http://dx.doi.org/10.1159/000487048
- ↑ Enemark EJ, Stenlund A, Joshua-Tor L. Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex. EMBO J. 2002 Mar 15;21(6):1487-96. PMID:11889054 doi:http://dx.doi.org/10.1093/emboj/21.6.1487