PMID- 10078529
OWN - NLM
STAT- MEDLINE
DCOM- 19990325
LR  - 20061115
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 398
IP  - 6722
DP  - 1999 Mar 4
TI  - Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue:
      implications for nuclear transport.
PG  - 39-46
AB  - The protein Ran is a small GTP-binding protein that binds to two types of
      effector inside the cell: Ran-binding proteins, which have a role in terminating 
      export processes from the nucleus to the cytoplasm, and importin-beta-like
      molecules that bind cargo proteins during nuclear transport. The Ran-binding
      domain is a conserved sequence motif found in several proteins that participate
      in these transport processes. The Ran-binding protein RanBP2 contains four of
      these domains and constitutes a large part of the cytoplasmic fibrils that extend
      from the nuclear-pore complex. The structure of Ran bound to a non-hydrolysable
      GTP analogue (Ran x GppNHp) in complex with the first Ran-binding domain (RanBD1)
      of human RanBP2 reveals not only that RanBD1 has a pleckstrin-homology domain
      fold, but also that the switch-I region of Ran x GppNHp resembles the canonical
      Ras GppNHp structure and that the carboxy terminus of Ran is wrapped around
      RanBD1, contacting a basic patch on RanBD1 through its acidic end. This molecular
      'embrace' enables RanBDs to sequester the Ran carboxy terminus, triggering the
      dissociation of Ran x GTP from importin-beta-related transport factors and
      facilitating GTP hydrolysis by the GTPase-activating protein ranGAP. Such a
      mechanism represents a new type of switch mechanism and regulatory
      protein-protein interaction for a Ras-related protein.
FAU - Vetter, I R
AU  - Vetter IR
AD  - Abteilung Strukturelle Biologie, Max-Planck-Institut fur molekulare Physiologie, 
      Dortmund, Germany.
FAU - Nowak, C
AU  - Nowak C
FAU - Nishimoto, T
AU  - Nishimoto T
FAU - Kuhlmann, J
AU  - Kuhlmann J
FAU - Wittinghofer, A
AU  - Wittinghofer A
LA  - eng
SI  - PDB/1RRP
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Blood Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Nuclear Pore Complex Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (platelet protein P47)
RN  - 0 (ran-binding protein 2)
RN  - 21820-51-9 (Phosphotyrosine)
RN  - 34273-04-6 (Guanylyl Imidodiphosphate)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (ran GTP-Binding Protein)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Biological Transport
MH  - Blood Proteins/chemistry
MH  - Cell Nucleus/*metabolism
MH  - Conserved Sequence
MH  - Crystallography, X-Ray
MH  - Cytoplasm/metabolism
MH  - DNA-Binding Proteins/chemistry/*metabolism
MH  - Escherichia coli
MH  - GTP-Binding Proteins/chemistry/*metabolism
MH  - Guanylyl Imidodiphosphate/chemistry/*metabolism
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Chaperones
MH  - Molecular Sequence Data
MH  - *Nuclear Pore Complex Proteins
MH  - Nuclear Proteins/chemistry/*metabolism
MH  - *Phosphoproteins
MH  - Phosphotyrosine/metabolism
MH  - Protein Binding
MH  - Protein Conformation
MH  - Recombinant Fusion Proteins/chemistry/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - ran GTP-Binding Protein
EDAT- 1999/03/17 03:05
MHDA- 2001/03/23 10:01
CRDT- 1999/03/17 03:05
PHST- 1999/03/17 03:05 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/03/17 03:05 [entrez]
AID - 10.1038/17969 [doi]
PST - ppublish
SO  - Nature. 1999 Mar 4;398(6722):39-46. doi: 10.1038/17969.