| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.66437639 |
| The refolded monoprenylated semisynthetic Rab 7 protein ( Rab7GG ) formed a stable complex with its natural chaperone REP 1 ( Rab escort protein 1 ) and could serve as an acceptor of the second prenyl group in the enzymatic prenylation reaction . 0.66437639^^^ |
|
| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.0 |
| Crystallization and preliminary 10 ray diffraction analysis of monoprenylated Rab 7 GTPase in complex with Rab escort protein 1 . ^^^ |
|
| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.0 |
| Moderate discrimination of REP 1 between Rab 7 10 GDP and Rab 7 10 GTP arises from a difference of an order of magnitude in dissociation rates . ^^^ The kinetics of the interaction of Rab 7 with REP 1 have been investigated using the fluorescence of GDP and GTP analogs at the active site of Rab 7 . ^^^ The results show that REP 1 has higher affinity for the GDP bound form of Rab 7 ( Kd=1 nM ) than for the GTP bound form ( Kd=20 nM ) . ^^^ |
|
| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.0 |
| Characterization of the ternary complex between Rab 7 , REP 1 and Rab geranylgeranyl transferase . ^^^ We demonstrate that the state of the nucleotide bound to Rab 7 does not influence the affinity of RabGGTase for the Rab 7 REP 1 complex . ^^^ Experiments using Rab 7 mutants in which the last 16 amino acids were either mutated or truncated revealed that the distal part of the C terminus makes only a limited contribution to the binding affinity between RabGGTase and the Rab 7 REP 1 complex . ^^^ |
|
| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.0 |
| Binding of the Rab 7 : REP 1 complex to GGTase 2 was found to be strongly modulated by geranylgeranyl pyrophosphate ( GGpp ) . ^^^ The affinity of GGTase 2 for the Rab 7 : REP 1 complex increases from ca . 120 nM to ca . 2 nM in the presence of GGpp . ^^^ Using this novel compound , we demonstrated that the affinity of doubly prenylated Rab 7 : REP 1 complex for GGTase 2 was 2 and 18 nM in the absence and presence of GGpp , respectively . ^^^ The affinity of GGpp for the prenylated Rab 7 : REP 1 : GGTase 2 was K ( d ) = 22 nM , with one molecule of GGpp binding per molecule of prenylated ternary complex . ^^^ In summary , these results demonstrate that GGpp acts as an allosteric activator that stabilizes the Rab 7 : REP 1 : GGTase 2 complex and triggers product release upon prenylation , preventing product inhibition of the enzyme . . ^^^ |
|
| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.0 |
| Purified monoprenylated REP 1 : Rab 7 was complexed with recombinant RabGGTase and crystallized in hanging drops . ^^^ |
|
| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.0 |
| Using this approach we generated fluorescent mono and diprenylated Rab 7 proteins that display near native properties and form stoichiometric complexes with their natural chaperone REP 1 . ^^^ We demonstrate that the complex formed from semisynthetic monoprenylated Rab 7 and REP 1 represents a genuine intermediate of the Rab prenylation reaction and thus provides a unique tool for studies of the Rab prenylation mechanism . ^^^ |
|
| Interacting proteins: P24386 and P51149 |
Pubmed |
SVM Score :0.0 |
| NA |
|