1tu3

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[[Image:1tu3.gif|left|200px]]<br /><applet load="1tu3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1tu3.gif|left|200px]]
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caption="1tu3, resolution 2.31&Aring;" />
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'''Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain'''<br />
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{{Structure
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|PDB= 1tu3 |SIZE=350|CAPTION= <scene name='initialview01'>1tu3</scene>, resolution 2.31&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene>
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|ACTIVITY=
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|GENE= RAB5A, RAB5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), RABEP1, RABPT5, RABPT5A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1TU3 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=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=1TU3 OCA].
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1TU3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU3 OCA].
==Reference==
==Reference==
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Structural basis of Rab5-Rabaptin5 interaction in endocytosis., Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC, Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15378032 15378032]
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Structural basis of Rab5-Rabaptin5 interaction in endocytosis., Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC, Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15378032 15378032]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: rabaptin5]]
[[Category: rabaptin5]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:23:10 2008''

Revision as of 12:23, 20 March 2008

Image:1tu3.gif


PDB ID 1tu3

Drag the structure with the mouse to rotate
, resolution 2.31Å
Ligands: and
Gene: RAB5A, RAB5 (Homo sapiens), RABEP1, RABPT5, RABPT5A (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Rab5 complex with Rabaptin5 C-terminal Domain


Overview

Rab5 is a small GTPase that regulates early endosome fusion. We present here the crystal structure of the Rab5 GTPase domain in complex with a GTP analog and the C-terminal domain of effector Rabaptin5. The proteins form a dyad-symmetric Rab5-Rabaptin5(2)-Rab5 ternary complex with a parallel coiled-coil Rabaptin5 homodimer in the middle. Two Rab5 molecules bind independently to the Rabaptin5 dimer using their switch and interswitch regions. The binding does not involve the Rab complementarity-determining regions. We also present the crystal structures of two distinct forms of GDP-Rab5 complexes, both of which are incompatible with Rabaptin5 binding. One has a dislocated and disordered switch I but a virtually intact switch II, whereas the other has its beta-sheet and both switch regions reorganized. Biochemical and functional analyses show that the crystallographically observed Rab5-Rabaptin5 complex also exists in solution, and disruption of this complex by mutation abrogates endosome fusion.

About this Structure

1TU3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of Rab5-Rabaptin5 interaction in endocytosis., Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC, Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. PMID:15378032

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