1DCQ
CRYSTAL STRUCTURE OF THE ARF-GAP DOMAIN AND ANKYRIN REPEATS OF PAPBETA.
Summary for 1DCQ
| Entry DOI | 10.2210/pdb1dcq/pdb |
| Descriptor | PYK2-ASSOCIATED PROTEIN BETA, ZINC ION (3 entities in total) |
| Functional Keywords | zinc-binding module, ankyrin repeats, metal binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm: Q7SIG6 |
| Total number of polymer chains | 1 |
| Total formula weight | 30954.69 |
| Authors | Mandiyan, V.,Andreev, J.,Schlessinger, J.,Hubbard, S.R. (deposition date: 1999-11-05, release date: 1999-12-22, Last modification date: 2024-10-09) |
| Primary citation | Mandiyan, V.,Andreev, J.,Schlessinger, J.,Hubbard, S.R. Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta. EMBO J., 18:6890-6898, 1999 Cited by PubMed Abstract: ADP ribosylation factors (ARFs), which are members of the Ras superfamily of GTP-binding proteins, are critical components of vesicular trafficking pathways in eukaryotes. Like Ras, ARFs are active in their GTP-bound form, and their duration of activity is controlled by GTPase-activating proteins (GAPs), which assist ARFs in hydrolyzing GTP to GDP. PAPbeta, a protein that binds to and is phosphorylated by the non-receptor tyrosine kinase PYK2, contains several modular signaling domains including a pleckstrin homology domain, an SH3 domain, ankyrin repeats and an ARF-GAP domain. Sequences of ARF-GAP domains show no recognizable similarity to those of other GAPs, and contain a characteristic Cys-X(2)-Cys-X(16-17)-Cys-X(2)-Cys motif. The crystal structure of the PAPbeta ARF-GAP domain and the C-terminal ankyrin repeats has been determined at 2.1 A resolution. The ARF-GAP domain comprises a central three-stranded beta-sheet flanked by five alpha-helices, with a Zn(2+) ion coordinated by the four cysteines of the cysteine-rich motif. Four ankyrin repeats are also present, the first two of which form an extensive interface with the ARF-GAP domain. An invariant arginine and several nearby hydrophobic residues are solvent exposed and are predicted to be the site of interaction with ARFs. Site-directed mutagenesis of these residues confirms their importance in ARF-GAP activity. PubMed: 10601011DOI: 10.1093/emboj/18.24.6890 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
