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- Publisher Website: 10.1016/j.bbrc.2019.05.050
- Scopus: eid_2-s2.0-85065407807
- PMID: 31092331
- WOS: WOS:000470803000065
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Article: Structural characterization of the redefined DNA-binding domain of human XPA
Title | Structural characterization of the redefined DNA-binding domain of human XPA |
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Authors | |
Keywords | X-ray crystallography DNA-Binding domain DNA repair Nucleotide excision repair Xeroderma pigmentosum complementation group A |
Issue Date | 2019 |
Publisher | Academic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description |
Citation | Biochemical and Biophysical Research Communications, 2019, v. 514 n. 3, p. 985-990 How to Cite? |
Abstract | XPA (xeroderma pigmentosum complementation group A), a key scaffold protein in nucleotide excision repair (NER) pathway, is important in DNA damage verification and repair proteins recruitment. Earlier studies had mapped the minimal DNA-binding domain (MBD) of XPA to a region corresponding to residues 98-219. However, recent studies indicated that the region involving residues 98-239 is the redefined DNA-binding domain (DBD), which binds to DNA substrates with a much higher binding affinity than MBD and possesses a nearly identical binding affinity to the full-length XPA protein. However, the structure of the redefined DBD domain of XPA (XPA-DBD) remains to be investigated. Here, we present the crystal structure of XPA-DBD at 2.06 Å resolution. Structure of the C-terminal region of XPA has been extended by 21 residues (Arg211-Arg231) as compared with previously reported MBD structures. The structure reveals that the C-terminal extension (Arg211-Arg231) is folded as an α-helix with multiple basic residues. The positively charged surface formed in the last C-terminal helix suggests its critical role in DNA binding. Further structural analysis demonstrates that the last C-terminal region (Asp217-Thr239) of XPA-DBD might undergo a conformational change to directly bind to the DNA substrates. This study provides a structural basis for understanding the possible mechanism of enhanced DNA-binding affinity of XPA-DBD. |
Persistent Identifier | http://hdl.handle.net/10722/278063 |
ISSN | 2023 Impact Factor: 2.5 2023 SCImago Journal Rankings: 0.770 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Lian, FM | - |
dc.contributor.author | Yang, X | - |
dc.contributor.author | Yang, W | - |
dc.contributor.author | Jiang, YL | - |
dc.contributor.author | Qian, C | - |
dc.date.accessioned | 2019-10-04T08:06:47Z | - |
dc.date.available | 2019-10-04T08:06:47Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Biochemical and Biophysical Research Communications, 2019, v. 514 n. 3, p. 985-990 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/10722/278063 | - |
dc.description.abstract | XPA (xeroderma pigmentosum complementation group A), a key scaffold protein in nucleotide excision repair (NER) pathway, is important in DNA damage verification and repair proteins recruitment. Earlier studies had mapped the minimal DNA-binding domain (MBD) of XPA to a region corresponding to residues 98-219. However, recent studies indicated that the region involving residues 98-239 is the redefined DNA-binding domain (DBD), which binds to DNA substrates with a much higher binding affinity than MBD and possesses a nearly identical binding affinity to the full-length XPA protein. However, the structure of the redefined DBD domain of XPA (XPA-DBD) remains to be investigated. Here, we present the crystal structure of XPA-DBD at 2.06 Å resolution. Structure of the C-terminal region of XPA has been extended by 21 residues (Arg211-Arg231) as compared with previously reported MBD structures. The structure reveals that the C-terminal extension (Arg211-Arg231) is folded as an α-helix with multiple basic residues. The positively charged surface formed in the last C-terminal helix suggests its critical role in DNA binding. Further structural analysis demonstrates that the last C-terminal region (Asp217-Thr239) of XPA-DBD might undergo a conformational change to directly bind to the DNA substrates. This study provides a structural basis for understanding the possible mechanism of enhanced DNA-binding affinity of XPA-DBD. | - |
dc.language | eng | - |
dc.publisher | Academic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description | - |
dc.relation.ispartof | Biochemical and Biophysical Research Communications | - |
dc.subject | X-ray crystallography | - |
dc.subject | DNA-Binding domain | - |
dc.subject | DNA repair | - |
dc.subject | Nucleotide excision repair | - |
dc.subject | Xeroderma pigmentosum complementation group A | - |
dc.title | Structural characterization of the redefined DNA-binding domain of human XPA | - |
dc.type | Article | - |
dc.identifier.email | Qian, C: cmqian@hku.hk | - |
dc.identifier.authority | Qian, C=rp01371 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.bbrc.2019.05.050 | - |
dc.identifier.pmid | 31092331 | - |
dc.identifier.scopus | eid_2-s2.0-85065407807 | - |
dc.identifier.hkuros | 306105 | - |
dc.identifier.volume | 514 | - |
dc.identifier.issue | 3 | - |
dc.identifier.spage | 985 | - |
dc.identifier.epage | 990 | - |
dc.identifier.isi | WOS:000470803000065 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 0006-291X | - |