1joc: Difference between revisions
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|PDB= 1joc |SIZE=350|CAPTION= <scene name='initialview01'>1joc</scene>, resolution 2.2Å | |PDB= 1joc |SIZE=350|CAPTION= <scene name='initialview01'>1joc</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |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= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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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==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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Merithew, E.]] | [[Category: Merithew, E.]] | ||
[[Category: Rajamani, D.]] | [[Category: Rajamani, D.]] | ||
[[Category: fyve domain]] | [[Category: fyve domain]] | ||
[[Category: inositol 3-phosphate binding]] | [[Category: inositol 3-phosphate binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:36:34 2008'' | ||
