1yhn

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(New page: 200px<br /> <applet load="1yhn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yhn, resolution 3.&Aring;" /> '''Structure basis of RI...)
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'''Structure basis of RILP recruitment by Rab7'''<br />
'''Structure basis of RILP recruitment by Rab7'''<br />
==Overview==
==Overview==
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Rab7 regulates vesicle traffic from early to late endosomes, and from late, endosomes to lysosomes. The crystal structure of Rab7-GTP in complex with, the Rab7 binding domain of RILP reveals that Rab7 interacts with RILP, specifically via two distinct areas, with the first one involving the, switch and interswitch regions and the second one consisting of RabSF1 and, RabSF4. Disruption of these interactions by mutations abrogates late, endosomal/lysosomal targeting of Rab7 and RILP. The Rab7 binding domain of, RILP forms a coiled-coil homodimer with two symmetric surfaces to interact, with two separate Rab7-GTP molecules, forming a dyad configuration of, Rab7-RILP(2)-Rab7. Mutations that disrupt RILP dimerization also abolish, its interactions with Rab7-GTP and late endosomal/lysosomal targeting, suggesting that the dimeric form of RILP is a functional unit. Structural, comparison suggests that the combined use of RabSF1 and RabSF4 with the, switch regions may be a general mode of action for most Rab proteins in, regulating membrane trafficking.
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Rab7 regulates vesicle traffic from early to late endosomes, and from late endosomes to lysosomes. The crystal structure of Rab7-GTP in complex with the Rab7 binding domain of RILP reveals that Rab7 interacts with RILP specifically via two distinct areas, with the first one involving the switch and interswitch regions and the second one consisting of RabSF1 and RabSF4. Disruption of these interactions by mutations abrogates late endosomal/lysosomal targeting of Rab7 and RILP. The Rab7 binding domain of RILP forms a coiled-coil homodimer with two symmetric surfaces to interact with two separate Rab7-GTP molecules, forming a dyad configuration of Rab7-RILP(2)-Rab7. Mutations that disrupt RILP dimerization also abolish its interactions with Rab7-GTP and late endosomal/lysosomal targeting, suggesting that the dimeric form of RILP is a functional unit. Structural comparison suggests that the combined use of RabSF1 and RabSF4 with the switch regions may be a general mode of action for most Rab proteins in regulating membrane trafficking.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1YHN 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 and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YHN OCA].
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1YHN 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> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YHN OCA].
==Reference==
==Reference==
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[[Category: rilp]]
[[Category: rilp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:19:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:23 2008''

Revision as of 14:05, 21 February 2008

Image:1yhn.gif

1yhn, resolution 3.Å

Drag the structure with the mouse to rotate

Structure basis of RILP recruitment by Rab7

Contents

Overview

Rab7 regulates vesicle traffic from early to late endosomes, and from late endosomes to lysosomes. The crystal structure of Rab7-GTP in complex with the Rab7 binding domain of RILP reveals that Rab7 interacts with RILP specifically via two distinct areas, with the first one involving the switch and interswitch regions and the second one consisting of RabSF1 and RabSF4. Disruption of these interactions by mutations abrogates late endosomal/lysosomal targeting of Rab7 and RILP. The Rab7 binding domain of RILP forms a coiled-coil homodimer with two symmetric surfaces to interact with two separate Rab7-GTP molecules, forming a dyad configuration of Rab7-RILP(2)-Rab7. Mutations that disrupt RILP dimerization also abolish its interactions with Rab7-GTP and late endosomal/lysosomal targeting, suggesting that the dimeric form of RILP is a functional unit. Structural comparison suggests that the combined use of RabSF1 and RabSF4 with the switch regions may be a general mode of action for most Rab proteins in regulating membrane trafficking.

Disease

Known disease associated with this structure: Charcot-Marie-Tooth disease, type 2B OMIM:[602298]

About this Structure

1YHN is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for recruitment of RILP by small GTPase Rab7., Wu M, Wang T, Loh E, Hong W, Song H, EMBO J. 2005 Apr 20;24(8):1491-501. Epub 2005 Mar 31. PMID:15933719

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