1ycj: Difference between revisions
New page: left|200px<br /><applet load="1ycj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ycj, resolution 1.95Å" /> '''Crystal structure of... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ycj.gif|left|200px]]<br /><applet load="1ycj" size=" | [[Image:1ycj.gif|left|200px]]<br /><applet load="1ycj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ycj, resolution 1.95Å" /> | caption="1ycj, resolution 1.95Å" /> | ||
'''Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate'''<br /> | '''Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate'''<br /> | ||
==Overview== | ==Overview== | ||
The X-ray structure of the ligand-binding core of the kainate receptor | The X-ray structure of the ligand-binding core of the kainate receptor GluR5 (GluR5-S1S2) in complex with (S)-glutamate was determined to 1.95 A resolution. The overall GluR5-S1S2 structure comprises two domains and is similar to the related AMPA receptor GluR2-S1S2J. (S)-glutamate binds as in GluR2-S1S2J. Distinct features are observed for Ser741, which stabilizes a highly coordinated network of water molecules and forms an interdomain bridge. The GluR5 complex exhibits a high degree of domain closure (26 degrees) relative to apo GluR2-S1S2J. In addition, GluR5-S1S2 forms a novel dimer interface with a different arrangement of the two protomers compared to GluR2-S1S2J. | ||
==About this Structure== | ==About this Structure== | ||
1YCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 and GLU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1YCJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GLU:'>GLU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCJ OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Egebjerg, J.]] | [[Category: Egebjerg, J.]] | ||
[[Category: Gajhede, M.]] | [[Category: Gajhede, M.]] | ||
[[Category: Kastrup, J | [[Category: Kastrup, J S.]] | ||
[[Category: Naur, P.]] | [[Category: Naur, P.]] | ||
[[Category: Skov, L | [[Category: Skov, L K.]] | ||
[[Category: Vestergaard, B.]] | [[Category: Vestergaard, B.]] | ||
[[Category: GLU]] | [[Category: GLU]] | ||
| Line 25: | Line 25: | ||
[[Category: kainate receptor]] | [[Category: kainate receptor]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:56 2008'' | ||
Revision as of 14:04, 21 February 2008
|
Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate
Overview
The X-ray structure of the ligand-binding core of the kainate receptor GluR5 (GluR5-S1S2) in complex with (S)-glutamate was determined to 1.95 A resolution. The overall GluR5-S1S2 structure comprises two domains and is similar to the related AMPA receptor GluR2-S1S2J. (S)-glutamate binds as in GluR2-S1S2J. Distinct features are observed for Ser741, which stabilizes a highly coordinated network of water molecules and forms an interdomain bridge. The GluR5 complex exhibits a high degree of domain closure (26 degrees) relative to apo GluR2-S1S2J. In addition, GluR5-S1S2 forms a novel dimer interface with a different arrangement of the two protomers compared to GluR2-S1S2J.
About this Structure
1YCJ is a Single protein structure of sequence from Rattus norvegicus with SO4 and GLU as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate., Naur P, Vestergaard B, Skov LK, Egebjerg J, Gajhede M, Kastrup JS, FEBS Lett. 2005 Feb 14;579(5):1154-60. PMID:15710405
Page seeded by OCA on Thu Feb 21 16:03:56 2008