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Cover Picture: NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein (ChemBioChem 2‐3/2003)
Author(s) -
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
Publication year - 2003
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200390021
Subject(s) - zinc finger , phd finger , lim domain , ring finger domain , zinc finger nuclease , zinc , chemistry , superman , crystallography , biology , biochemistry , genetics , gene , transcription factor , organic chemistry
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.