We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1h6i

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1h6i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h6i, resolution 3.54&Aring;" /> '''A REFINED STRUCTURE...)
Line 1: Line 1:
-
[[Image:1h6i.gif|left|200px]]<br />
+
[[Image:1h6i.gif|left|200px]]<br /><applet load="1h6i" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1h6i" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1h6i, resolution 3.54&Aring;" />
caption="1h6i, resolution 3.54&Aring;" />
'''A REFINED STRUCTURE OF HUMAN AQUAPORIN 1'''<br />
'''A REFINED STRUCTURE OF HUMAN AQUAPORIN 1'''<br />
==Overview==
==Overview==
-
A refined structure of the human water channel aquaporin-1 is presented., The model rests on the high resolution X-ray structure of the homologous, bacterial glycerol transporter GlpF, electron crystallographic data at 3.8, A resolution and a multiple sequence alignment of the aquaporin, superfamily. The crystallographic R and free R values (36.7% and 37.8%), for the refined structure are significantly lower than for previous, models. Improved geometry and enhanced stability in molecular dynamics, simulations demonstrate a significant improvement of the aquaporin-1, structure. Comparison with previous aquaporin-1 models shows significant, differences, not only in the loop regions, but also in the core of the, water channel.
+
A refined structure of the human water channel aquaporin-1 is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter GlpF, electron crystallographic data at 3.8 A resolution and a multiple sequence alignment of the aquaporin superfamily. The crystallographic R and free R values (36.7% and 37.8%) for the refined structure are significantly lower than for previous models. Improved geometry and enhanced stability in molecular dynamics simulations demonstrate a significant improvement of the aquaporin-1 structure. Comparison with previous aquaporin-1 models shows significant differences, not only in the loop regions, but also in the core of the water channel.
==Disease==
==Disease==
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
1H6I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H6I OCA].
+
1H6I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6I OCA].
==Reference==
==Reference==
Line 18: Line 17:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Engel, A.]]
[[Category: Engel, A.]]
-
[[Category: Groot, B.L.De.]]
+
[[Category: Groot, B L.De.]]
[[Category: Grubmuller, H.]]
[[Category: Grubmuller, H.]]
[[Category: electron diffraction]]
[[Category: electron diffraction]]
Line 26: Line 25:
[[Category: water channel]]
[[Category: water channel]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:13:23 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:56 2008''

Revision as of 10:57, 21 February 2008


1h6i, resolution 3.54Å

Drag the structure with the mouse to rotate

A REFINED STRUCTURE OF HUMAN AQUAPORIN 1

Contents

Overview

A refined structure of the human water channel aquaporin-1 is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter GlpF, electron crystallographic data at 3.8 A resolution and a multiple sequence alignment of the aquaporin superfamily. The crystallographic R and free R values (36.7% and 37.8%) for the refined structure are significantly lower than for previous models. Improved geometry and enhanced stability in molecular dynamics simulations demonstrate a significant improvement of the aquaporin-1 structure. Comparison with previous aquaporin-1 models shows significant differences, not only in the loop regions, but also in the core of the water channel.

Disease

Known diseases associated with this structure: Aquaporin-1 deficiency OMIM:[107776], Blood group, Colton OMIM:[107776]

About this Structure

1H6I is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A refined structure of human aquaporin-1., de Groot BL, Engel A, Grubmuller H, FEBS Lett. 2001 Aug 31;504(3):206-11. PMID:11532455

Page seeded by OCA on Thu Feb 21 12:57:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools