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The zinc finger motif Conservation of chemical shifts and correlation with structure
Author(s) -
Lee Min S.,
Mortishire-Smith Russell J.,
Wright Peter E.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80732-v
Subject(s) - zinc finger , zinc , chemical shift , chemistry , cysteine , histidine , structural motif , crystallography , stereochemistry , biochemistry , transcription factor , amino acid , gene , enzyme , organic chemistry
Zinc fingers of the transcription factor IIIA (TFIIIA) type, in which zinc is co‐ordinated by two cysteine and two histidine ligands (Cys 2 /His 2 ), contain a length of helix packed against a β‐hairpin. These zinc fingers comprise the wider range of structurally homologous proteins for which 1 H chemical shifts are available. A number of key resonances have chemical shifts that are highly sensitive to tertiary structure and are conserved between these peptides. The high conservation of these fingerprint chemical shifts is correlated with the common global fold of Cys 2 /His 2 zinc fingers. These chemical shifts are largely independent of primary structure and should facilitate NMR assignments for future zinc finger proteins, as well as provide a diagnostic signature for the characteristic Cys 2 /His 2 zinc finger fold.