A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure.
Nup475 (also known as tristetraprolin and TIS11) includes two zinc-binding domains of the form Cys-X8-Cys-X5-Cys-X3-His. These domains are required for rapid degradation of tumor necrosis factor (TNF) and other mRNAs through the interaction with AU-rich elements in their 3'-untranslated regions. The three-dimensional solution structure of the first domain was determined by multidimensional nuclear magnetic resonance spectroscopy, revealing a novel fold around a central zinc ion. The core structure is disk-like with a diameter of approximately 25 A and a width of approximately 12 A. This structure provides a basis for evaluating the role of individual residues for structural stability and for nucleic acid binding.
Amann
Barbara T
BT
Department of Biophysics and Biophysical Chemistry, 713 WBSB, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.
Worthington
Mark T
MT
Berg
Jeremy M
JM
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics; D000818:Animals; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry*; D004268:DNA-Binding Proteins; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D017874:Immediate-Early Proteins / Q000737:chemistry* / Q000235:genetics; D051379:Mice; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding / Q000235:genetics; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000235:genetics; D012996:Solutions; D051816:Tristetraprolin; D016335:Zinc Fingers / Q000235:genetics
D004268:DNA-Binding Proteins; D017874:Immediate-Early Proteins; D012996:Solutions; D051816:Tristetraprolin; C497552:ZFP36 protein, human; C497553:Zfp36 protein, mouse; D006639:Histidine; D003545:Cysteine