PMID- 10655614
OWN - NLM
STAT- MEDLINE
DCOM- 20000303
LR  - 20121115
IS  - 1072-8368 (Print)
IS  - 1072-8368 (Linking)
VI  - 7
IP  - 2
DP  - 2000 Feb
TI  - The Rac-RhoGDI complex and the structural basis for the regulation of Rho
      proteins by RhoGDI.
PG  - 122-6
AB  - Rho family-specific guanine nucleotide dissociation inhibitors (RhoGDIs) decrease
      the rate of nucleotide dissociation and release Rho proteins such as RhoA, Rac
      and Cdc42 from membranes, forming tight complexes that shuttle between cytosol
      and membrane compartments. We have solved the crystal structure of a complex
      between the RhoGDI homolog LyGDI and GDP-bound Rac2, which are abundant in
      leukocytes, representing the cytosolic, resting pool of Rho species to be
      activated by extracellular signals. The N-terminal domain of LyGDI (LyN), which
      has been reported to be flexible in isolated RhoGDIs, becomes ordered upon
      complex formation and contributes more than 60% to the interface area. The
      structure is consistent with the C-terminus of Rac2 binding to a hydrophobic
      cavity previously proposed as isoprenyl binding site. An inner segment of LyN
      forms a helical hairpin that contacts mainly the switch regions of Rac2. The
      architecture of the complex interface suggests a mechanism for the inhibition of 
      guanine nucleotide dissociation that is based on the stabilization of the
      magnesium (Mg2+) ion in the nucleotide binding pocket.
FAU - Scheffzek, K
AU  - Scheffzek K
AD  - Max-Planck-Institut fur molekulare Physiologie, Abteilung Strukturelle Biologie, 
      Otto-Hahn-Str. 11, 44227 Dortmund, Germany. klaus@mpimf-heidelberg.mpg.de
FAU - Stephan, I
AU  - Stephan I
FAU - Jensen, O N
AU  - Jensen ON
FAU - Illenberger, D
AU  - Illenberger D
FAU - Gierschik, P
AU  - Gierschik P
LA  - eng
SI  - PDB/1DS6
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Nat Struct Biol
JT  - Nature structural biology
JID - 9421566
RN  - 0 (GDP dissociation inhibitor 1)
RN  - 0 (Guanine Nucleotide Dissociation Inhibitors)
RN  - 0 (Proteins)
RN  - 0 (rho-Specific Guanine Nucleotide Dissociation Inhibitors)
RN  - 146-91-8 (Guanosine Diphosphate)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - EC 3.6.1.- (rac2 GTP-binding protein)
RN  - EC 3.6.5.2 (rac GTP-Binding Proteins)
RN  - EC 3.6.5.2 (rho GTP-Binding Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Cell Membrane/metabolism
MH  - Crystallography, X-Ray
MH  - Guanine Nucleotide Dissociation Inhibitors/*chemistry/*metabolism
MH  - Guanosine Diphosphate/chemistry/metabolism
MH  - Guanosine Triphosphate/metabolism
MH  - Hydrolysis
MH  - Lipid Metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Proteins/chemistry/metabolism
MH  - rac GTP-Binding Proteins/*chemistry/*metabolism
MH  - rho GTP-Binding Proteins/chemistry/metabolism
MH  - rho-Specific Guanine Nucleotide Dissociation Inhibitors
EDAT- 2000/02/03 09:00
MHDA- 2000/03/11 09:00
CRDT- 2000/02/03 09:00
PHST- 2000/02/03 09:00 [pubmed]
PHST- 2000/03/11 09:00 [medline]
PHST- 2000/02/03 09:00 [entrez]
AID - 10.1038/72392 [doi]
PST - ppublish
SO  - Nat Struct Biol. 2000 Feb;7(2):122-6. doi: 10.1038/72392.