1joc

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(New page: 200px<br /> <applet load="1joc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1joc, resolution 2.2&Aring;" /> '''EEA1 homodimer of C-...)
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[[Image:1joc.gif|left|200px]]<br />
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[[Image:1joc.gif|left|200px]]<br /><applet load="1joc" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1joc" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1joc, resolution 2.2&Aring;" />
caption="1joc, resolution 2.2&Aring;" />
'''EEA1 homodimer of C-terminal FYVE domain bound to inositol 1,3-diphosphate'''<br />
'''EEA1 homodimer of C-terminal FYVE domain bound to inositol 1,3-diphosphate'''<br />
==Overview==
==Overview==
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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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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1JOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and ITP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1JOC with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb87_1.html Zinc Fingers]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JOC OCA].
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1JOC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ITP:'>ITP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1JOC with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb87_1.html Zinc Fingers]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JOC OCA].
==Reference==
==Reference==
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[[Category: Zinc Fingers]]
[[Category: Zinc Fingers]]
[[Category: Corvera, S.]]
[[Category: Corvera, S.]]
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[[Category: Dumas, J.J.]]
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[[Category: Dumas, J J.]]
[[Category: Hayes, S.]]
[[Category: Hayes, S.]]
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[[Category: Lambright, D.G.]]
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[[Category: Lambright, D G.]]
[[Category: Lawe, D.]]
[[Category: Lawe, D.]]
[[Category: Merithew, E.]]
[[Category: Merithew, E.]]
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[[Category: inositol 3-phosphate binding]]
[[Category: inositol 3-phosphate binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:43:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:50 2008''

Revision as of 11:24, 21 February 2008


1joc, resolution 2.2Å

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

Contents

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.

Disease

Known disease associated with this structure: Spastic paraplegia 33 OMIM:[610243]

About this Structure

1JOC is a Single protein structure of sequence from Homo sapiens with and as ligands. 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

Page seeded by OCA on Thu Feb 21 13:24:50 2008

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