PMID- 10601011
OWN - NLM
STAT- MEDLINE
DCOM- 20000127
LR  - 20121115
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 24
DP  - 1999 Dec 15
TI  - Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated
      protein beta.
PG  - 6890-8
AB  - 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.
FAU - Mandiyan, V
AU  - Mandiyan V
AD  - Department of Pharmacology, Skirball Institute of Biomolecular Medicine, New York
      University Medical School, New York, NY 10016, USA.
FAU - Andreev, J
AU  - Andreev J
FAU - Schlessinger, J
AU  - Schlessinger J
FAU - Hubbard, S R
AU  - Hubbard SR
LA  - eng
SI  - PDB/1DCQ
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Ankyrins)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Focal Adhesion Kinase 2)
RN  - EC 3.6.5.2 (ADP-Ribosylation Factors)
SB  - IM
MH  - ADP-Ribosylation Factors/*chemistry/metabolism
MH  - Amino Acid Sequence
MH  - Ankyrins/*chemistry/metabolism
MH  - Catalysis
MH  - Computer Graphics
MH  - Crystallography, X-Ray/methods
MH  - Focal Adhesion Kinase 2
MH  - Kinetics
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Protein Structure, Secondary
MH  - Protein-Tyrosine Kinases/*chemistry/*metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Repetitive Sequences, Amino Acid
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - src Homology Domains
PMC - PMC1171752
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1093/emboj/18.24.6890 [doi]
PST - ppublish
SO  - EMBO J. 1999 Dec 15;18(24):6890-8. doi: 10.1093/emboj/18.24.6890.