1gv4
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Mitochondria play a key role in apoptosis due to their capacity to release | + | Mitochondria play a key role in apoptosis due to their capacity to release potentially lethal proteins. One of these latent death factors is cytochrome c, which can stimulate the proteolytic activation of caspase zymogens. Another important protein is apoptosis-inducing factor (AIF), a flavoprotein that can stimulate a caspase-independent cell-death pathway required for early embryonic morphogenesis. Here, we report the crystal structure of mouse AIF at 2.0 A. Its active site structure and redox properties suggest that AIF functions as an electron transferase with a mechanism similar to that of the bacterial ferredoxin reductases, its closest evolutionary homologs. However, AIF structurally differs from these proteins in some essential features, including a long insertion in a C-terminal beta-hairpin loop, which may be related to its apoptogenic functions. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alzari, P | + | [[Category: Alzari, P M.]] |
| - | [[Category: Mate, M | + | [[Category: Mate, M J.]] |
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: apoptosi]] | [[Category: apoptosi]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:19 2008'' |
Revision as of 10:54, 21 February 2008
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MURINE APOPTOSIS-INDUCING FACTOR (AIF)
Overview
Mitochondria play a key role in apoptosis due to their capacity to release potentially lethal proteins. One of these latent death factors is cytochrome c, which can stimulate the proteolytic activation of caspase zymogens. Another important protein is apoptosis-inducing factor (AIF), a flavoprotein that can stimulate a caspase-independent cell-death pathway required for early embryonic morphogenesis. Here, we report the crystal structure of mouse AIF at 2.0 A. Its active site structure and redox properties suggest that AIF functions as an electron transferase with a mechanism similar to that of the bacterial ferredoxin reductases, its closest evolutionary homologs. However, AIF structurally differs from these proteins in some essential features, including a long insertion in a C-terminal beta-hairpin loop, which may be related to its apoptogenic functions.
About this Structure
1GV4 is a Single protein structure of sequence from Mus musculus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The crystal structure of the mouse apoptosis-inducing factor AIF., Mate MJ, Ortiz-Lombardia M, Boitel B, Haouz A, Tello D, Susin SA, Penninger J, Kroemer G, Alzari PM, Nat Struct Biol. 2002 Jun;9(6):442-6. PMID:11967568
Page seeded by OCA on Thu Feb 21 12:54:19 2008
Categories: Mus musculus | Single protein | Alzari, P M. | Mate, M J. | FAD | Apoptosi | Fad | Flavoprotein | Nuclear protein | Oxidoreductase
