2c08
From Proteopedia
(New page: 200px<br /><applet load="2c08" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c08, resolution 2.90Å" /> '''RAT ENDOPHILIN A1 BA...) |
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| - | [[Image:2c08.gif|left|200px]]<br /><applet load="2c08" size=" | + | [[Image:2c08.gif|left|200px]]<br /><applet load="2c08" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2c08, resolution 2.90Å" /> | caption="2c08, resolution 2.90Å" /> | ||
'''RAT ENDOPHILIN A1 BAR DOMAIN'''<br /> | '''RAT ENDOPHILIN A1 BAR DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Endophilin-A1 is a BAR domain-containing protein enriched at synapses and | + | Endophilin-A1 is a BAR domain-containing protein enriched at synapses and is implicated in synaptic vesicle endocytosis. It binds to dynamin and synaptojanin via a C-terminal SH3 domain. We examine the mechanism by which the BAR domain and an N-terminal amphipathic helix, which folds upon membrane binding, work as a functional unit (the N-BAR domain) to promote dimerisation and membrane curvature generation. By electron paramagnetic resonance spectroscopy, we show that this amphipathic helix is peripherally bound in the plane of the membrane, with the midpoint of insertion aligned with the phosphate level of headgroups. This places the helix in an optimal position to effect membrane curvature generation. We solved the crystal structure of rat endophilin-A1 BAR domain and examined a distinctive insert protruding from the membrane interaction face. This insert is predicted to form an additional amphipathic helix and is important for curvature generation. Its presence defines an endophilin/nadrin subclass of BAR domains. We propose that N-BAR domains function as low-affinity dimers regulating binding partner recruitment to areas of high membrane curvature. |
==About this Structure== | ==About this Structure== | ||
| - | 2C08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 2C08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C08 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Evans, P | + | [[Category: Evans, P R.]] |
| - | [[Category: Gallop, J | + | [[Category: Gallop, J L.]] |
| - | [[Category: Kent, H | + | [[Category: Kent, H M.]] |
| - | [[Category: Mcmahon, H | + | [[Category: Mcmahon, H T.]] |
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
[[Category: bar domain]] | [[Category: bar domain]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:32 2008'' |
Revision as of 14:43, 21 February 2008
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RAT ENDOPHILIN A1 BAR DOMAIN
Overview
Endophilin-A1 is a BAR domain-containing protein enriched at synapses and is implicated in synaptic vesicle endocytosis. It binds to dynamin and synaptojanin via a C-terminal SH3 domain. We examine the mechanism by which the BAR domain and an N-terminal amphipathic helix, which folds upon membrane binding, work as a functional unit (the N-BAR domain) to promote dimerisation and membrane curvature generation. By electron paramagnetic resonance spectroscopy, we show that this amphipathic helix is peripherally bound in the plane of the membrane, with the midpoint of insertion aligned with the phosphate level of headgroups. This places the helix in an optimal position to effect membrane curvature generation. We solved the crystal structure of rat endophilin-A1 BAR domain and examined a distinctive insert protruding from the membrane interaction face. This insert is predicted to form an additional amphipathic helix and is important for curvature generation. Its presence defines an endophilin/nadrin subclass of BAR domains. We propose that N-BAR domains function as low-affinity dimers regulating binding partner recruitment to areas of high membrane curvature.
About this Structure
2C08 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Mechanism of endophilin N-BAR domain-mediated membrane curvature., Gallop JL, Jao CC, Kent HM, Butler PJ, Evans PR, Langen R, McMahon HT, EMBO J. 2006 Jun 21;25(12):2898-910. Epub 2006 Jun 8. PMID:16763559
Page seeded by OCA on Thu Feb 21 16:43:32 2008
