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| - | [[Image:1z0j.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1z0j.png|left|200px]] |
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| | {{STRUCTURE_1z0j| PDB=1z0j | SCENE= }} | | {{STRUCTURE_1z0j| PDB=1z0j | SCENE= }} |
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| - | '''Structure of GTP-Bound Rab22Q64L GTPase in complex with the minimal Rab binding domain of Rabenosyn-5'''
| + | ===Structure of GTP-Bound Rab22Q64L GTPase in complex with the minimal Rab binding domain of Rabenosyn-5=== |
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| - | ==Overview==
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| - | Rab GTPases regulate all stages of membrane trafficking, including vesicle budding, cargo sorting, transport, tethering and fusion. In the inactive (GDP-bound) conformation, accessory factors facilitate the targeting of Rab GTPases to intracellular compartments. After nucleotide exchange to the active (GTP-bound) conformation, Rab GTPases interact with functionally diverse effectors including lipid kinases, motor proteins and tethering complexes. How effectors distinguish between homologous Rab GTPases represents an unresolved problem with respect to the specificity of vesicular trafficking. Using a structural proteomic approach, we have determined the specificity and structural basis underlying the interaction of the multivalent effector rabenosyn-5 with the Rab family. The results demonstrate that even the structurally similar effector domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions. The observed specificity is determined at a family-wide level by structural diversity in the active conformation, which governs the spatial disposition of critical conserved recognition determinants, and by a small number of both positive and negative sequence determinants that allow further discrimination between Rab GTPases with similar switch conformations.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16034420}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16034420 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16034420}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rab22 gtpase]] | | [[Category: Rab22 gtpase]] |
| | [[Category: Rabenosyn]] | | [[Category: Rabenosyn]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:02:22 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:30:02 2008'' |
Revision as of 18:30, 28 July 2008
Template:STRUCTURE 1z0j
Structure of GTP-Bound Rab22Q64L GTPase in complex with the minimal Rab binding domain of Rabenosyn-5
Template:ABSTRACT PUBMED 16034420
About this Structure
1Z0J is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis of family-wide Rab GTPase recognition by rabenosyn-5., Eathiraj S, Pan X, Ritacco C, Lambright DG, Nature. 2005 Jul 21;436(7049):415-9. PMID:16034420
Page seeded by OCA on Mon Jul 28 21:30:02 2008
