1joc

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|PDB= 1joc |SIZE=350|CAPTION= <scene name='initialview01'>1joc</scene>, resolution 2.2&Aring;
|PDB= 1joc |SIZE=350|CAPTION= <scene name='initialview01'>1joc</scene>, resolution 2.2&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ITP:PHOSPHORIC ACID MONO-(2,3,4,6-TETRAHYDROXY-5-PHOSPHONOOXY-CYCLOHEXYL) ESTER'>ITP</scene>
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|LIGAND= <scene name='pdbligand=ITP:PHOSPHORIC+ACID+MONO-(2,3,4,6-TETRAHYDROXY-5-PHOSPHONOOXY-CYCLOHEXYL)+ESTER'>ITP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1joc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1joc OCA], [http://www.ebi.ac.uk/pdbsum/1joc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1joc RCSB]</span>
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}}
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==Overview==
==Overview==
Early endosome autoantigen localization to early endosomes is mediated by a C-terminal region, which includes a calmodulin binding motif, a Rab5 interaction site, and a FYVE domain that selectively binds phosphatidyl inositol 3-phosphate. The crystal structure of the C-terminal region bound to inositol 1,3-bisphosphate reveals an organized, quaternary assembly consisting of a parallel coiled coil and a dyad-symmetric FYVE domain homodimer. Structural and biochemical observations support a multivalent mechanism for endosomal localization in which domain organization, dimerization, and quaternary structure amplify the weak affinity and modest specificity of head group interactions with conserved residues. A unique mode of membrane engagement deduced from the quaternary structure of the C-terminal region provides insight into the structural basis of endosome tethering.
Early endosome autoantigen localization to early endosomes is mediated by a C-terminal region, which includes a calmodulin binding motif, a Rab5 interaction site, and a FYVE domain that selectively binds phosphatidyl inositol 3-phosphate. The crystal structure of the C-terminal region bound to inositol 1,3-bisphosphate reveals an organized, quaternary assembly consisting of a parallel coiled coil and a dyad-symmetric FYVE domain homodimer. Structural and biochemical observations support a multivalent mechanism for endosomal localization in which domain organization, dimerization, and quaternary structure amplify the weak affinity and modest specificity of head group interactions with conserved residues. A unique mode of membrane engagement deduced from the quaternary structure of the C-terminal region provides insight into the structural basis of endosome tethering.
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==Disease==
 
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Known disease associated with this structure: Spastic paraplegia 33 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=610243 610243]]
 
==About this Structure==
==About this Structure==
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[[Category: Merithew, E.]]
[[Category: Merithew, E.]]
[[Category: Rajamani, D.]]
[[Category: Rajamani, D.]]
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[[Category: ITP]]
 
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[[Category: ZN]]
 
[[Category: fyve domain]]
[[Category: fyve domain]]
[[Category: inositol 3-phosphate binding]]
[[Category: inositol 3-phosphate binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:06:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:36:34 2008''

Revision as of 18:36, 30 March 2008


PDB ID 1joc

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



EEA1 homodimer of C-terminal FYVE domain bound to inositol 1,3-diphosphate


Overview

Early endosome autoantigen localization to early endosomes is mediated by a C-terminal region, which includes a calmodulin binding motif, a Rab5 interaction site, and a FYVE domain that selectively binds phosphatidyl inositol 3-phosphate. The crystal structure of the C-terminal region bound to inositol 1,3-bisphosphate reveals an organized, quaternary assembly consisting of a parallel coiled coil and a dyad-symmetric FYVE domain homodimer. Structural and biochemical observations support a multivalent mechanism for endosomal localization in which domain organization, dimerization, and quaternary structure amplify the weak affinity and modest specificity of head group interactions with conserved residues. A unique mode of membrane engagement deduced from the quaternary structure of the C-terminal region provides insight into the structural basis of endosome tethering.

About this Structure

1JOC is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1JOC with [Zinc Fingers]. Full crystallographic information is available from OCA.

Reference

Multivalent endosome targeting by homodimeric EEA1., Dumas JJ, Merithew E, Sudharshan E, Rajamani D, Hayes S, Lawe D, Corvera S, Lambright DG, Mol Cell. 2001 Nov;8(5):947-58. PMID:11741531

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