2d57

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2d57" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d57, resolution 3.20&Aring;" /> '''Double layered 2D cr...)
Line 1: Line 1:
-
[[Image:2d57.gif|left|200px]]<br /><applet load="2d57" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2d57.gif|left|200px]]<br /><applet load="2d57" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2d57, resolution 3.20&Aring;" />
caption="2d57, resolution 3.20&Aring;" />
'''Double layered 2D crystal structure of AQUAPORIN-4 (AQP4M23) at 3.2 a resolution by electron crystallography'''<br />
'''Double layered 2D crystal structure of AQUAPORIN-4 (AQP4M23) at 3.2 a resolution by electron crystallography'''<br />
==Overview==
==Overview==
-
Aquaporin-4 (AQP4) is the predominant water channel in the mammalian brain, and an important drug target for treatment of cerebral edema, bipolar, disorder and mesial temporal lobe epilepsy. We determined the AQP4, structure by electron crystallography of double-layered, two-dimensional, (2D) crystals. The structure allows us to discuss how the expression ratio, between the long and short AQP4 splicing variant can determine the size of, in vivo orthogonal arrays. Furthermore, AQP4 contains a short 3(10) helix, in an extracellular loop, which mediates weak but specific interactions, between AQP4 molecules in adjoining membranes. This finding suggests a, previously unexpected role for AQP4 in cell adhesion. This notion was, corroborated by expression of AQP4 in L-cells, which resulted in, clustering of the cells. Our AQP4 structure thus enables us to propose, models for the size regulation of orthogonal arrays and channel-mediated, cell adhesion.
+
Aquaporin-4 (AQP4) is the predominant water channel in the mammalian brain and an important drug target for treatment of cerebral edema, bipolar disorder and mesial temporal lobe epilepsy. We determined the AQP4 structure by electron crystallography of double-layered, two-dimensional (2D) crystals. The structure allows us to discuss how the expression ratio between the long and short AQP4 splicing variant can determine the size of in vivo orthogonal arrays. Furthermore, AQP4 contains a short 3(10) helix in an extracellular loop, which mediates weak but specific interactions between AQP4 molecules in adjoining membranes. This finding suggests a previously unexpected role for AQP4 in cell adhesion. This notion was corroborated by expression of AQP4 in L-cells, which resulted in clustering of the cells. Our AQP4 structure thus enables us to propose models for the size regulation of orthogonal arrays and channel-mediated cell adhesion.
==About this Structure==
==About this Structure==
-
2D57 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D57 OCA].
+
2D57 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=2D57 OCA].
==Reference==
==Reference==
Line 34: Line 34:
[[Category: water transport]]
[[Category: water transport]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:26:58 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:29 2008''

Revision as of 14:55, 21 February 2008

Image:2d57.gif

2d57, resolution 3.20Å

Drag the structure with the mouse to rotate

Double layered 2D crystal structure of AQUAPORIN-4 (AQP4M23) at 3.2 a resolution by electron crystallography

Overview

Aquaporin-4 (AQP4) is the predominant water channel in the mammalian brain and an important drug target for treatment of cerebral edema, bipolar disorder and mesial temporal lobe epilepsy. We determined the AQP4 structure by electron crystallography of double-layered, two-dimensional (2D) crystals. The structure allows us to discuss how the expression ratio between the long and short AQP4 splicing variant can determine the size of in vivo orthogonal arrays. Furthermore, AQP4 contains a short 3(10) helix in an extracellular loop, which mediates weak but specific interactions between AQP4 molecules in adjoining membranes. This finding suggests a previously unexpected role for AQP4 in cell adhesion. This notion was corroborated by expression of AQP4 in L-cells, which resulted in clustering of the cells. Our AQP4 structure thus enables us to propose models for the size regulation of orthogonal arrays and channel-mediated cell adhesion.

About this Structure

2D57 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Implications of the aquaporin-4 structure on array formation and cell adhesion., Hiroaki Y, Tani K, Kamegawa A, Gyobu N, Nishikawa K, Suzuki H, Walz T, Sasaki S, Mitsuoka K, Kimura K, Mizoguchi A, Fujiyoshi Y, J Mol Biol. 2006 Jan 27;355(4):628-39. Epub 2005 Nov 17. PMID:16325200

Page seeded by OCA on Thu Feb 21 16:55:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d57"
Personal tools