Cover Picture: NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein (ChemBioChem 2-3/2003)

The cover picture shows the NMR structure of the SUPERMAN zinc finger domain, which is the first high‐resolution structure of a classical zinc finger domain from a plant protein. The structure consists of a very well‐defined ββα motif, typical of all the other Cys 2 –His 2 zinc fingers so far struct...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2003-03, Vol.4 (2-3), p.125-125
Main Authors: Isernia, Carla, Bucci, Enrico, Leone, Marilisa, Zaccaro, Laura, Di Lello, Paola, Digilio, Giuseppe, Esposito, Sabrina, Saviano, Michele, Di Blasio, Benedetto, Pedone, Carlo, Pedone, Paolo V., Fattorusso, Roberto
Format: Article
Language:English
Subjects:
DNA recognition
NMR spectroscopy
structure elucidation
SUPERMAN
zinc finger domain
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Summary:The cover picture shows the NMR structure of the SUPERMAN zinc finger domain, which is the first high‐resolution structure of a classical zinc finger domain from a plant protein. The structure consists of a very well‐defined ββα motif, typical of all the other Cys 2 –His 2 zinc fingers so far structurally characterized. As a consequence, the QALGGH sequence, which is highly conserved in plant protein classical zinc finger domains, is located at the N terminus of the α helix. Interestingly, this domain region, in animal protein zinc fingers, is constituted of hypervariable residues deputed to the recognition of the DNA bases. Therefore, a peculiar DNA recognition code for the QALGGH zinc finger domain is proposed in the article by Fattorusso and co‐workers on p. 171 ff.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200390021