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1h6i
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6i OCA], [http://www.ebi.ac.uk/pdbsum/1h6i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h6i RCSB]</span> | ||
}} | }} | ||
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==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== | ||
| - | Known diseases associated with this structure: Aquaporin-1 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107776 107776]], Blood group, Colton OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107776 107776]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: water channel]] | [[Category: water channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:46 2008'' |
Revision as of 17:58, 30 March 2008
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| , resolution 3.54Å | |||||||
|---|---|---|---|---|---|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A REFINED STRUCTURE OF HUMAN AQUAPORIN 1
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.
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 Sun Mar 30 20:58:46 2008
