2eta
From Proteopedia
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| - | [[Image:2eta.gif|left|200px]] | + | [[Image:2eta.gif|left|200px]] |
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| - | '''Crystal structure of the ankyrin repeat domain of the TRPV2''' | + | {{Structure |
| + | |PDB= 2eta |SIZE=350|CAPTION= <scene name='initialview01'>2eta</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Trpv2, Sac2b, Vrl1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the ankyrin repeat domain of the TRPV2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2ETA is a [ | + | 2ETA 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=2ETA OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel., Jin X, Touhey J, Gaudet R, J Biol Chem. 2006 Sep 1;281(35):25006-10. Epub 2006 Jun 29. PMID:[http:// | + | Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel., Jin X, Touhey J, Gaudet R, J Biol Chem. 2006 Sep 1;281(35):25006-10. Epub 2006 Jun 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16809337 16809337] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trpv2]] | [[Category: trpv2]] | ||
| - | ''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 16:44:07 2008'' |
Revision as of 14:44, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Gene: | Trpv2, Sac2b, Vrl1 (Rattus norvegicus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the ankyrin repeat domain of the TRPV2
Overview
The TRPV ion channels mediate responses to many sensory stimuli including heat, low pH, neuropeptides, and chemical ligands. All TRPV subfamily members contain an intracellular N-terminal ankyrin repeat domain (ARD), a prevalent protein interaction motif. The 1.6-A crystal structure of the TRPV2-ARD, with six ankyrin repeats, reveals several atypical structural features. Repeats one through three display unusually long and flexible fingers with a large number of exposed aromatic residues, whereas repeats five and six have unusually long outer helices. Furthermore, a large counterclockwise twist observed in the stacking of repeats four and five breaks the regularity of the domain, altering the shape of surfaces available for interactions with proteins or other cellular ligands. Both solution studies and crystal packing interactions indicate that the TRPV2-ARD does not form homo-oligomers, suggesting that the ARD of TRPV ion channels may be used for interactions with regulatory factors rather than in promoting tetrameric assembly of the ion channels.
About this Structure
2ETA is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel., Jin X, Touhey J, Gaudet R, J Biol Chem. 2006 Sep 1;281(35):25006-10. Epub 2006 Jun 29. PMID:16809337
Page seeded by OCA on Thu Mar 20 16:44:07 2008
