PMID- 10025402
OWN - NLM
STAT- MEDLINE
DCOM- 19990303
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 96
IP  - 3
DP  - 1999 Feb 5
TI  - Structural basis of Rab effector specificity: crystal structure of the small G
      protein Rab3A complexed with the effector domain of rabphilin-3A.
PG  - 363-74
AB  - The small G protein Rab3A plays an important role in the regulation of
      neurotransmitter release. The crystal structure of activated Rab3A/GTP/Mg2+ bound
      to the effector domain of rabphilin-3A was solved to 2.6 A resolution.
      Rabphilin-3A contacts Rab3A in two distinct areas. The first interface involves
      the Rab3A switch I and switch II regions, which are sensitive to the
      nucleotide-binding state of Rab3A. The second interface consists of a deep pocket
      in Rab3A that interacts with a SGAWFF structural element of rabphilin-3A.
      Sequence and structure analysis, and biochemical data suggest that this pocket,
      or Rab complementarity-determining region (RabCDR), establishes a specific
      interaction between each Rab protein and its effectors. RabCDRs could be major
      determinants of effector specificity during vesicle trafficking and fusion.
FAU - Ostermeier, C
AU  - Ostermeier C
AD  - The Howard Hughes Medical Institute and Department of Molecular Biophysics and
      Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
FAU - Brunger, A T
AU  - Brunger AT
LA  - eng
SI  - PDB/1ZBD
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Vesicular Transport Proteins)
RN  - 0 (rabphilin-3A)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (rab GTP-Binding Proteins)
RN  - EC 3.6.5.2 (rab3 GTP-Binding Proteins)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Cattle
MH  - Crystallization
MH  - Crystallography, X-Ray
MH  - Dimerization
MH  - GTP-Binding Proteins/*chemistry/isolation & purification
MH  - Humans
MH  - Macromolecular Substances
MH  - Mice
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*chemistry/isolation & purification
MH  - Peptide Fragments/chemistry/isolation & purification
MH  - Protein Structure, Tertiary
MH  - Proto-Oncogene Proteins/*chemistry/isolation & purification
MH  - Rats
MH  - Vesicular Transport Proteins
MH  - *rab GTP-Binding Proteins
MH  - rab3 GTP-Binding Proteins
EDAT- 1999/02/20 00:00
MHDA- 1999/02/20 00:01
CRDT- 1999/02/20 00:00
PHST- 1999/02/20 00:00 [pubmed]
PHST- 1999/02/20 00:01 [medline]
PHST- 1999/02/20 00:00 [entrez]
AID - S0092-8674(00)80549-8 [pii]
AID - 10.1016/s0092-8674(00)80549-8 [doi]
PST - ppublish
SO  - Cell. 1999 Feb 5;96(3):363-74. doi: 10.1016/s0092-8674(00)80549-8.