1z06: Difference between revisions
New page: left|200px<br /><applet load="1z06" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z06, resolution 1.81Å" /> '''GppNHp-Bound Rab33 G... |
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[[Image:1z06.gif|left|200px]]<br /><applet load="1z06" size=" | [[Image:1z06.gif|left|200px]]<br /><applet load="1z06" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1z06, resolution 1.81Å" /> | caption="1z06, resolution 1.81Å" /> | ||
'''GppNHp-Bound Rab33 GTPase'''<br /> | '''GppNHp-Bound Rab33 GTPase'''<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== | ||
1Z06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1Z06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z06 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[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 16:10:54 2008'' | ||
Revision as of 17:10, 21 February 2008
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GppNHp-Bound Rab33 GTPase
OverviewOverview
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 StructureAbout this Structure
1Z06 is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
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