2gf5
From Proteopedia
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| - | [[Image:2gf5.gif|left|200px]] | + | [[Image:2gf5.gif|left|200px]] |
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| - | '''Structure of intact FADD (MORT1)''' | + | {{Structure |
| + | |PDB= 2gf5 |SIZE=350|CAPTION= <scene name='initialview01'>2gf5</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= FADD, MORT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of intact FADD (MORT1)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GF5 is a [ | + | 2GF5 is a [[Single protein]] structure of sequence 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=2GF5 OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of FADD and its mode of interaction with procaspase-8., Carrington PE, Sandu C, Wei Y, Hill JM, Morisawa G, Huang T, Gavathiotis E, Wei Y, Werner MH, Mol Cell. 2006 Jun 9;22(5):599-610. PMID:[http:// | + | The structure of FADD and its mode of interaction with procaspase-8., Carrington PE, Sandu C, Wei Y, Hill JM, Morisawa G, Huang T, Gavathiotis E, Wei Y, Werner MH, Mol Cell. 2006 Jun 9;22(5):599-610. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16762833 16762833] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: death-inducing signaling complex]] | [[Category: death-inducing signaling complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:03:55 2008'' |
Revision as of 15:03, 20 March 2008
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| Gene: | FADD, MORT1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of intact FADD (MORT1)
Overview
The structure of FADD has been solved in solution, revealing that the death effector domain (DED) and death domain (DD) are aligned with one another in an orthogonal, tail-to-tail fashion. Mutagenesis of FADD and functional reconstitution with its binding partners define the interaction with the intracellular domain of CD95 and the prodomain of procaspase-8 and reveal a self-association surface necessary to form a productive complex with an activated "death receptor." The identification of a procaspase-specific binding surface on the FADD DED suggests a preferential interaction with one, but not both, of the DEDs of procaspase-8 in a perpendicular arrangement. FADD self-association is mediated by a "hydrophobic patch" in the vicinity of F25 in the DED. The structure of FADD and its functional characterization, therefore, illustrate the architecture of key components in the death-inducing signaling complex.
About this Structure
2GF5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of FADD and its mode of interaction with procaspase-8., Carrington PE, Sandu C, Wei Y, Hill JM, Morisawa G, Huang T, Gavathiotis E, Wei Y, Werner MH, Mol Cell. 2006 Jun 9;22(5):599-610. PMID:16762833
Page seeded by OCA on Thu Mar 20 17:03:55 2008
