@article{
 title = {A class of zinc fingers involved in protein-protein interactions: biophysical characterization of CCHC fingers from FOG and U-shaped},
 type = {article},
 year = {2000},
 identifiers = {[object Object]},
 pages = {1030-1038},
 volume = {267},
 id = {c0ff378c-3636-32e4-9c81-4cc7f7bee61a},
 created = {2020-08-14T07:45:07.861Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {c2dc1a38-fc29-3f20-8d91-e4e1a13d85ae},
 last_modified = {2020-10-01T04:11:25.614Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Matthews2000a},
 source_type = {Journal Article},
 notes = {COPYRIGHT 2000 ACS<br/>CAPLUS<br/>AN 2000:155047<br/>6<br/>General Biochemistry<br/>Department of Biochemistry,University of Sydney,Australia.<br/>Journal<br/>EJBCAI<br/>written in English.},
 private_publication = {false},
 abstract = {Zinc fingers (ZnFs) are extremely common protein domains. Several classes of ZnFs are distinguished by the nature and spacing of their zinc-coordinating residues. While the structure and function of some ZnFs are well characterized, many others have been identified only through their amino acid sequence. A no. of proteins contain a conserved C-X2-C-X12-H-X1-5-C sequence, which is similar to the spacing obsd. for the \"classic\" CCHH ZnFs. Although these domains have been implicated in protein-protein (and not protein-nucleic acid) interactions, nothing is known about their structure or function at a mol. level. Here, we address this problem through the expression and biophys. characterization of several CCHC-type zinc fingers from the erythroid transcription factor FOG and the related Drosophila protein U-shaped. Each of these domains does indeed fold in a zinc-dependent fashion, coordinating the metal in a tetrahedral manner through the sidechains of one histidine and three cysteine residues, and forming extremely thermostable structures. Anal. of CD spectra suggests an overall fold similar to that of the CCHH fingers, and indeed a point mutant of FOG-F1 in which the final cysteine residue is replaced by histidine remains capable of folding. However, the CCHC (as opposed to CCHH) motif is a prerequisite for GATA-1 binding activity, demonstrating that CCHC and CCHH topologies are not interchangeable. This demonstration that members of a structurally distinct subclass of genuine zinc finger domains are involved in the mediation of protein-protein interactions has implications for the prediction of protein function from nucleotide sequences.},
 bibtype = {article},
 author = {Matthews, Jacqueline M and Kowalski, Kasper and Liew, Chu Kong and Sharpe, Belinda K and Fox, Archa H and Crossley, Merlin and Mackay, Joel P},
 journal = {Eur. J. Biochem.},
 number = {4}
}

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Several classes of ZnFs are distinguished by the nature and spacing of their zinc-coordinating residues. While the structure and function of some ZnFs are well characterized, many others have been identified only through their amino acid sequence. A no. of proteins contain a conserved C-X2-C-X12-H-X1-5-C sequence, which is similar to the spacing obsd. for the \\\"classic\\\" CCHH ZnFs. Although these domains have been implicated in protein-protein (and not protein-nucleic acid) interactions, nothing is known about their structure or function at a mol. level. Here, we address this problem through the expression and biophys. characterization of several CCHC-type zinc fingers from the erythroid transcription factor FOG and the related Drosophila protein U-shaped. Each of these domains does indeed fold in a zinc-dependent fashion, coordinating the metal in a tetrahedral manner through the sidechains of one histidine and three cysteine residues, and forming extremely thermostable structures. Anal. of CD spectra suggests an overall fold similar to that of the CCHH fingers, and indeed a point mutant of FOG-F1 in which the final cysteine residue is replaced by histidine remains capable of folding. However, the CCHC (as opposed to CCHH) motif is a prerequisite for GATA-1 binding activity, demonstrating that CCHC and CCHH topologies are not interchangeable. 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