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1j4n

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Crystal Structure of the AQP1 water channel

Structural highlights

1j4n is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AQP1_BOVIN Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Water channels facilitate the rapid transport of water across cell membranes in response to osmotic gradients. These channels are believed to be involved in many physiological processes that include renal water conservation, neuro-homeostasis, digestion, regulation of body temperature and reproduction. Members of the water channel superfamily have been found in a range of cell types from bacteria to human. In mammals, there are currently 10 families of water channels, referred to as aquaporins (AQP): AQP0-AQP9. Here we report the structure of the aquaporin 1 (AQP1) water channel to 2.2 A resolution. The channel consists of three topological elements, an extracellular and a cytoplasmic vestibule connected by an extended narrow pore or selectivity filter. Within the selectivity filter, four bound waters are localized along three hydrophilic nodes, which punctuate an otherwise extremely hydrophobic pore segment. This unusual combination of a long hydrophobic pore and a minimal number of solute binding sites facilitates rapid water transport. Residues of the constriction region, in particular histidine 182, which is conserved among all known water-specific channels, are critical in establishing water specificity. Our analysis of the AQP1 pore also indicates that the transport of protons through this channel is highly energetically unfavourable.

Structural basis of water-specific transport through the AQP1 water channel.,Sui H, Han BG, Lee JK, Walian P, Jap BK Nature. 2001 Dec 20-27;414(6866):872-8. PMID:11780053^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sui H, Han BG, Lee JK, Walian P, Jap BK. Structural basis of water-specific transport through the AQP1 water channel. Nature. 2001 Dec 20-27;414(6866):872-8. PMID:11780053 doi:10.1038/414872a

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j4n"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the AQP1 water channel==
-<StructureSection load='1j4n' size='340' side='right' caption='[[1j4n]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='1j4n' size='340' side='right'caption='[[1j4n]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1j4n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J4N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1j4n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J4N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fqy|1fqy]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4n OCA], [http://pdbe.org/1j4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j4n RCSB], [http://www.ebi.ac.uk/pdbsum/1j4n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j4n ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j4n OCA], [https://pdbe.org/1j4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j4n RCSB], [https://www.ebi.ac.uk/pdbsum/1j4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j4n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AQP1_BOVIN AQP1_BOVIN]] Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.
+[https://www.uniprot.org/uniprot/AQP1_BOVIN AQP1_BOVIN] Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 </div>
 <div class="pdbe-citations 1j4n" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Aquaporin 3D structures|Aquaporin 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 37: @@
 </StructureSection>
 [[Category: Bos taurus]]
-[[Category: Han, B G]]
+[[Category: Large Structures]]
-[[Category: Jap, B K]]
+[[Category: Han B-G]]
-[[Category: Lee, J K]]
+[[Category: Jap BK]]
-[[Category: Sui, H]]
+[[Category: Lee JK]]
-[[Category: Walian, P]]
+[[Category: Sui H]]
-[[Category: Channel protein]]
+[[Category: Walian P]]
-[[Category: Membrane protein]]
-[[Category: Transmembrane helice]]

1j4n

From Proteopedia

Current revision

Crystal Structure of the AQP1 water channel

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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