1z0k
From Proteopedia
(New page: 200px<br /> <applet load="1z0k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z0k, resolution 1.92Å" /> '''Structure of GTP-Bo...) |
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| - | [[Image:1z0k.gif|left|200px]]<br /> | + | [[Image:1z0k.gif|left|200px]]<br /><applet load="1z0k" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1z0k" size=" | + | |
caption="1z0k, resolution 1.92Å" /> | caption="1z0k, resolution 1.92Å" /> | ||
'''Structure of GTP-Bound Rab4Q67L GTPase in complex with the central Rab binding domain of Rabenosyn-5'''<br /> | '''Structure of GTP-Bound Rab4Q67L GTPase in complex with the central Rab binding domain of Rabenosyn-5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rab GTPases regulate all stages of membrane trafficking, including vesicle | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z0K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, GTP and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1Z0K is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GTP:'>GTP</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0K OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Eathiraj, S.]] | [[Category: Eathiraj, S.]] | ||
| - | [[Category: Lambright, D | + | [[Category: Lambright, D G.]] |
[[Category: Pan, X.]] | [[Category: Pan, X.]] | ||
[[Category: Ritacco, C.]] | [[Category: Ritacco, C.]] | ||
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[[Category: vesicular trafficking]] | [[Category: vesicular trafficking]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:58 2008'' |
Revision as of 14:10, 21 February 2008
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Structure of GTP-Bound Rab4Q67L GTPase in complex with the central Rab binding domain of Rabenosyn-5
Overview
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.
About this Structure
1Z0K is a Protein complex structure of sequences from Homo sapiens with , and as ligands. 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 Thu Feb 21 16:10:58 2008
Categories: Homo sapiens | Protein complex | Eathiraj, S. | Lambright, D G. | Pan, X. | Ritacco, C. | GTP | MES | MG | Effector complex | Protein transport | Rab gtpases | Rab4 | Rabenosyn | Vesicular trafficking
