2c08
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2c08.gif|left|200px]] | + | [[Image:2c08.gif|left|200px]] |
| - | + | ||
| - | '''RAT ENDOPHILIN A1 BAR DOMAIN''' | + | {{Structure |
| + | |PDB= 2c08 |SIZE=350|CAPTION= <scene name='initialview01'>2c08</scene>, resolution 2.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''RAT ENDOPHILIN A1 BAR DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2C08 is a [ | + | 2C08 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16763559 16763559] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 28: | Line 37: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 16:09:04 2008'' |
Revision as of 14:09, 20 March 2008
| |||||||
| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 16:09:04 2008
