PF00641

Zn-finger in Ran binding protein and others

Pfam entry
Member databasePfam
Pfam typedomain
Short namezf-RanBP
ClanZn_Beta_Ribbon
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description
Imported from IPR001876

This entry represents the zinc finger domain found in RanBP2 proteins. Ran is an evolutionary conserved member of the Ras superfamily that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Ran binding protein 2 (RanBP2) is a 358kDa nucleoporin located on the cytoplasmic side of the nuclear pore complex which plays a role in nuclear protein import
[7]
. RanBP2 contains multiple zinc fingers which mediate binding to RanGDP
[6]
.

Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates
[1, 2, 3, 4, 8]
. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few
[5]
. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.

References
Imported from IPR001876

1.Zinc finger peptides for the regulation of gene expression. Klug A. J. Mol. Biol. 293, 215-8, (1999). View articlePMID: 10529348

2.Multiple modes of RNA recognition by zinc finger proteins. Hall TM. Curr. Opin. Struct. Biol. 15, 367-73, (2005). View articlePMID: 15963892

3.Zinc finger proteins: getting a grip on RNA. Brown RS. Curr. Opin. Struct. Biol. 15, 94-8, (2005). View articlePMID: 15718139

4.Sticky fingers: zinc-fingers as protein-recognition motifs. Gamsjaeger R, Liew CK, Loughlin FE, Crossley M, Mackay JP. Trends Biochem. Sci. 32, 63-70, (2007). View articlePMID: 17210253

5.Zinc finger proteins: new insights into structural and functional diversity. Laity JH, Lee BM, Wright PE. Curr. Opin. Struct. Biol. 11, 39-46, (2001). View articlePMID: 11179890

6.Two distinct classes of Ran-binding sites on the nucleoporin Nup-358. Yaseen NR, Blobel G. Proc. Natl. Acad. Sci. U.S.A. 96, 5516-21, (1999). View articlePMID: 10318915

7.Regulation of nuclear import and export by the GTPase Ran. Steggerda SM, Paschal BM. Int. Rev. Cytol. 217, 41-91, (2002). View articlePMID: 12019565

8.Zinc fingers--folds for many occasions. Matthews JM, Sunde M. IUBMB Life 54, 351-5, (2002). View articlePMID: 12665246

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