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Zinc fingers as protein recognition motifs: structural basis for the GATA-1/Friend of GATA interaction
Structural highlights
FunctionGATA1_MOUSE Transcriptional activator which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence [AT]GATA[AG] within regulatory regions of globin genes and of other genes expressed in erythroid cells.[1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGATA-1 and friend of GATA (FOG) are zinc-finger transcription factors that physically interact to play essential roles in erythroid and megakaryocytic development. Several naturally occurring mutations in the GATA-1 gene that alter the FOG-binding domain have been reported. The mutations are associated with familial anemias and thrombocytopenias of differing severity. To elucidate the molecular basis for the GATA-1/FOG interaction, we have determined the three-dimensional structure of a complex comprising the interaction domains of these proteins. The structure reveals how zinc fingers can act as protein recognition motifs. Details of the architecture of the contact domains and their physical properties provide a molecular explanation for how the GATA-1 mutations contribute to distinct but related genetic diseases. Zinc fingers as protein recognition motifs: structural basis for the GATA-1/friend of GATA interaction.,Liew CK, Simpson RJ, Kwan AH, Crofts LA, Loughlin FE, Matthews JM, Crossley M, Mackay JP Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):583-8. Epub 2005 Jan 11. PMID:15644435[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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