1ih5
From Proteopedia
(Difference between revisions)
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- | + | ==CRYSTAL STRUCTURE OF AQUAPORIN-1== | |
- | === | + | <StructureSection load='1ih5' size='340' side='right' caption='[[1ih5]], [[Resolution|resolution]] 3.70Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[1ih5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hw0 1hw0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IH5 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ih5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ih5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ih5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ih5 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/1ih5_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The water-selective pathway through the aquaporin-1 membrane channel has been visualized by fitting an atomic model to a 3.7-A resolution three-dimensional density map. This map was determined by analyzing images and electron diffraction patterns of lipid-reconstituted two-dimensional crystals of aquaporin-1 preserved in vitrified buffer in the absence of any additive. The aqueous pathway is characterized by a size-selective pore that is approximately 4.0 +/- 0.5A in diameter, spans a length of approximately 18A, and bends by approximately 25 degrees as it traverses the bilayer. This narrow pore is connected by wide, funnel-shaped openings at the extracellular and cytoplasmic faces. The size-selective pore is outlined mostly by hydrophobic residues, resulting in a relatively inert pathway conducive to diffusion-limited water flow. The apex of the curved pore is close to the locations of the in-plane pseudo-2-fold symmetry axis that relates the N- and C-terminal halves and the conserved, functionally important N76 and N192 residues. | ||
- | + | Visualization of a water-selective pore by electron crystallography in vitreous ice.,Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1398-403. Epub 2001 Jan 30. PMID:11171962<ref>PMID:11171962</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
*[[Aquaporin|Aquaporin]] | *[[Aquaporin|Aquaporin]] | ||
- | + | *[[Aquaporin-1|Aquaporin-1]] | |
- | == | + | == References == |
- | < | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Cheng, A.]] | [[Category: Cheng, A.]] |
Revision as of 16:40, 29 September 2014
CRYSTAL STRUCTURE OF AQUAPORIN-1
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