Abstract
Background: Classical zinc finger proteins are extremely abundant and interact with DNA using a well defined recognition code. Results: We solved the structure of ZNF217 bound to its cognate DNA. Conclusion: ZNF217 presents a unique DNA interaction pattern including a new type of protein-DNA contact. Significance: This study deepens our understanding of DNA recognition by classical zinc fingers.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 10616-10627 |
| Number of pages | 12 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 15 |
| DOIs | |
| State | Published - Apr 12 2013 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
Cite this
New insights into DNA recognition by zinc fingers revealed by structural analysis of the oncoprotein ZNF217. / Vandevenne, Marylène; Jacques, David A.; Artuz, Crisbel; Nguyen, Cuong Dinh; Kwan, Ann H Y; Segal, David; Matthews, Jacqueline M.; Crossley, Merlin; Guss, J. Mitchell; MacKay, Joel P.
In: Journal of Biological Chemistry, Vol. 288, No. 15, 12.04.2013, p. 10616-10627.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - New insights into DNA recognition by zinc fingers revealed by structural analysis of the oncoprotein ZNF217
AU - Vandevenne, Marylène
AU - Jacques, David A.
AU - Artuz, Crisbel
AU - Nguyen, Cuong Dinh
AU - Kwan, Ann H Y
AU - Segal, David
AU - Matthews, Jacqueline M.
AU - Crossley, Merlin
AU - Guss, J. Mitchell
AU - MacKay, Joel P.
PY - 2013/4/12
Y1 - 2013/4/12
N2 - Background: Classical zinc finger proteins are extremely abundant and interact with DNA using a well defined recognition code. Results: We solved the structure of ZNF217 bound to its cognate DNA. Conclusion: ZNF217 presents a unique DNA interaction pattern including a new type of protein-DNA contact. Significance: This study deepens our understanding of DNA recognition by classical zinc fingers.
AB - Background: Classical zinc finger proteins are extremely abundant and interact with DNA using a well defined recognition code. Results: We solved the structure of ZNF217 bound to its cognate DNA. Conclusion: ZNF217 presents a unique DNA interaction pattern including a new type of protein-DNA contact. Significance: This study deepens our understanding of DNA recognition by classical zinc fingers.
UR - http://www.scopus.com/inward/record.url?scp=84876238286&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84876238286&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.441451
DO - 10.1074/jbc.M112.441451
M3 - Article
C2 - 23436653
AN - SCOPUS:84876238286
VL - 288
SP - 10616
EP - 10627
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 15
ER -