3U9G: Crystal Structure Of The Zinc Finger Antiviral Protein

Zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses, such as HIV-1, by targeting viral mRNA for degradation. How ZAP recognizes its target RNA has been unclear. Here we report the crystal structure of the N-terminal domain of rat ZAP (NZAP225), the major functional domain. The overall structure of NZAP225 resembles a tractor, with four zinc-finger motifs located at the bottom. Structural and functional analyses identified multiple positively charged residues and two putative RNA-binding cavities forming a large putative RNA-binding cleft. ZAP molecules interact to form a dimer that binds to a ZAP-responsive RNA molecule containing two ZAP-binding modules. These results provide insights into how ZAP binds specifically to complex target RNA.
PDB ID: 3U9GDownload
MMDB ID: 97970
PDB Deposition Date: 2011/10/18
Updated in MMDB: 2013/07
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3U9G: monomeric; determined by author
Molecular Components in 3U9G
Label Count Molecule
Protein (1 molecule)
Zinc Finger Ccch-type Antiviral Protein 1(Gene symbol: Zc3hav1)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB