|PROSITE documentation PDOC50119 [for PROSITE entry PS50119]|
The B-box zinc finger is an around 40 amino acids domain. One or two copies of this motif are generally associated with a RING finger and a coiled coil motif to form the so-called tripartite motif. It is found essentially in transcription factors, ribonucleoproteins and proto-oncoproteins, but no function is clearly assigned to this domain . It has been shown to be essential but not sufficient to localize the PML protein in a punctate pattern in interphase nuclei .
Among the 7 possible ligands for the zinc atom contained in a B-box, only 4 are used and bind one zinc atom in a Cys2-His2 tetrahedral arrangement. The NMR analysis reveals that the B-box structure comprises two β-strands, two helical turns and three extended loop regions different from any other zinc binding motif .
Proteins currently known to include the zinc finger B-box domain are listed below:
We developed a profile that covers the whole domain.Last update:
December 2001 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||RING fingers and B-boxes: zinc-binding protein-protein interaction domains.|
|Source||Biochem. Cell Biol. 76:351-358(1998).|
|2||Authors||Borden K.L. Lally J.M. Martin S.R. O'Reilly N.J. Solomon E. Freemont P.S.|
|Title||In vivo and in vitro characterization of the B1 and B2 zinc-binding domains from the acute promyelocytic leukemia protooncoprotein PML.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 93:1601-1606(1996).|
|3||Authors||Borden K.L. Lally J.M. Martin S.R. O'Reilly N.J. Etkin L.D. Freemont P.S.|
|Title||Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development.|
|Source||EMBO J. 14:5947-5956(1995).|