Zinc fingers, zinc clusters, and zinc twists in DNA-binding protein domains

Journal Article · Fri Feb 01 00:00:00 EST 1991 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.88.3.999· OSTI ID:5012951

Vallee, B L; Auld, D S ^[1]; Coleman, J E ^[2]

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1. Harvard Medical School, Boston, MA (United States)
2. Yale Univ., New Haven, CT (United States)

The authors recognize three distinct motifs of DNA-binding zinc proteins: (i) zinc fingers, (ii) zinc clusters, and (iii) zinc twists. Until very recently, x-ray crystallographic or NMR three-dimensional structure analyses of DNA-binding zinc proteins have not been available to serve as standards of reference for the zinc binding sites of these families of proteins. Those of the DNA-binding domains of the fungal transcription factor GAL4 and the rat glucocorticoid receptor are the first to have been determined. Both proteins contain two zinc binding sites, and in both, cysteine residues are the sole zinc ligands. In GAL4, two zinc atoms are bound to six cysteine residues which form a zinc cluster akin to that of metallothionein; the distance between the two zinc atoms of GAL4 is {approximately}3.5{angstrom}. In the glucocorticoid receptor, each zinc atom is bound to four cysteine residues; the interatomic zinc-zinc distance is {approximately}13{angstrom}, and in this instance, a zinc twist is represented by a helical DNA recognition site located between the two zinc atoms. Zinc clusters and zinc twists are here recognized as two distinctive motifs in DNA-binding proteins containing multiple zinc atoms. For native zinc fingers, structural data do not exist as yet; consequently, the interatomic distances between zinc atoms are not known. As further structural data become available, the structural and functional significance of these different motifs in their binding to DNA and other proteins participating in the transmission of the genetic message will become apparent.

• OSTI ID: 5012951
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 88:3; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
METALLOPROTEINS
X-RAY DIFFRACTION
TRANSCRIPTION FACTORS
NUCLEAR MAGNETIC RESONANCE
CADMIUM 113
CRYSTALLOGRAPHY
CYSTEINE
LIGANDS
PROTONS
ZINC COMPOUNDS
AMINO ACIDS
BARYONS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CADMIUM ISOTOPES
CARBOXYLIC ACIDS
COHERENT SCATTERING
DIFFRACTION
ELEMENTARY PARTICLES
EVEN-ODD NUCLEI
FERMIONS
HADRONS
INTERMEDIATE MASS NUCLEI
INTERNAL CONVERSION RADIOISOTOPES
ISOMERIC TRANSITION ISOTOPES
ISOTOPES
MAGNETIC RESONANCE
NUCLEI
NUCLEONS
NUCLEOPROTEINS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PROTEINS
RADIOISOTOPES
RESONANCE
SCATTERING
STABLE ISOTOPES
THIOLS
YEARS LIVING RADIOISOTOPES
550601* - Medicine- Unsealed Radionuclides in Diagnostics