1ih5

From Proteopedia

(Difference between revisions)

Revision as of 07:42, 7 April 2021

CRYSTAL STRUCTURE OF AQUAPORIN-1

Structural highlights

1ih5 is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1hw0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AQP1_HUMAN] 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.^[1]

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

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^[2]

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

References

↑ Preston GM, Carroll TP, Guggino WB, Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 1992 Apr 17;256(5055):385-7. PMID:1373524
↑ Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK. Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1398-403. Epub 2001 Jan 30. PMID:11171962 doi:10.1073/pnas.041489198

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/1ih5"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ih5' size='340' side='right'caption='[[1ih5]], [[Resolution|resolution]] 3.70&Aring;' 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>
+<table><tr><td colspan='2'>[[1ih5]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1IH5 FirstGlance]. <br>
-</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=1ih5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ih5 OCA], [http://pdbe.org/1ih5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ih5 RCSB], [http://www.ebi.ac.uk/pdbsum/1ih5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ih5 ProSAT]</span></td></tr>
+</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=1ih5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ih5 OCA], [https://pdbe.org/1ih5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ih5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ih5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ih5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AQP1_HUMAN AQP1_HUMAN]] 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.<ref>PMID:1373524</ref>
+[[https://www.uniprot.org/uniprot/AQP1_HUMAN AQP1_HUMAN]] 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.<ref>PMID:1373524</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
 *[[Aquaporin 3D structures|Aquaporin 3D structures]]
-*[[Aquaporin-1|Aquaporin-1]]
 == References ==
 <references/>

1ih5

From Proteopedia

Revision as of 07:42, 7 April 2021

CRYSTAL STRUCTURE OF AQUAPORIN-1

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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