7wlu: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='7wlu' size='340' side='right'caption='[[7wlu]], [[Resolution|resolution]] 6.81&Aring;' scene=''>
<StructureSection load='7wlu' size='340' side='right'caption='[[7wlu]], [[Resolution|resolution]] 6.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7wlu]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WLU FirstGlance]. <br>
<table><tr><td colspan='2'>[[7wlu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WLU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLX:(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL'>PLX</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLX:(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL'>PLX</scene></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=7wlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wlu OCA], [https://pdbe.org/7wlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wlu RCSB], [https://www.ebi.ac.uk/pdbsum/7wlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wlu 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=7wlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wlu OCA], [https://pdbe.org/7wlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wlu RCSB], [https://www.ebi.ac.uk/pdbsum/7wlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wlu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PIEZ1_MOUSE PIEZ1_MOUSE]] Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology.<ref>PMID:20813920</ref> <ref>PMID:22343900</ref> <ref>PMID:24157948</ref> <ref>PMID:24958852</ref> <ref>PMID:25119035</ref> 
[[https://www.uniprot.org/uniprot/PIEZ1_MOUSE PIEZ1_MOUSE]] Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology.<ref>PMID:20813920</ref> <ref>PMID:22343900</ref> <ref>PMID:24157948</ref> <ref>PMID:24958852</ref> <ref>PMID:25119035</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PIEZO channels respond to piconewton-scale forces to mediate critical physiological and pathophysiological processes(1-5). Detergent-solubilized PIEZO channels form bowl-shaped trimers comprising a central ion-conducting pore with an extracellular cap and three curved and non-planar blades with intracellular beams(6-10), which may undergo force-induced deformation within lipid membranes(11). However, the structures and mechanisms underlying the gating dynamics of PIEZO channels in lipid membranes remain unresolved. Here we determine the curved and flattened structures of PIEZO1 reconstituted in liposome vesicles, directly visualizing the substantial deformability of the PIEZO1-lipid bilayer system and an in-plane areal expansion of approximately 300 nm(2) in the flattened structure. The curved structure of PIEZO1 resembles the structure determined from detergent micelles, but has numerous bound phospholipids. By contrast, the flattened structure exhibits membrane tension-induced flattening of the blade, bending of the beam and detaching and rotating of the cap, which could collectively lead to gating of the ion-conducting pathway. On the basis of the measured in-plane membrane area expansion and stiffness constant of PIEZO1 (ref. (11)), we calculate a half maximal activation tension of about 1.9 pN nm(-1), matching experimentally measured values. Thus, our studies provide a fundamental understanding of how the notable deformability and structural rearrangement of PIEZO1 achieve exquisite mechanosensitivity and unique curvature-based gating in lipid membranes.
 
Structure deformation and curvature sensing of PIEZO1 in lipid membranes.,Yang X, Lin C, Chen X, Li S, Li X, Xiao B Nature. 2022 Apr;604(7905):377-383. doi: 10.1038/s41586-022-04574-8. Epub 2022, Apr 6. PMID:35388220<ref>PMID:35388220</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wlu" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 23: Line 14:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, X]]
[[Category: Mus musculus]]
[[Category: Li, S]]
[[Category: Chen X]]
[[Category: Li, X]]
[[Category: Li S]]
[[Category: Lin, C]]
[[Category: Li X]]
[[Category: Xiao, B]]
[[Category: Lin C]]
[[Category: Yang, X]]
[[Category: Xiao B]]
[[Category: Complex]]
[[Category: Yang X]]
[[Category: Flexible]]
[[Category: Force]]
[[Category: Membrane protein]]

Latest revision as of 10:25, 8 September 2022

The Flattened Structure of mPIEZO1 in Lipid BilayerThe Flattened Structure of mPIEZO1 in Lipid Bilayer

Structural highlights

7wlu is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PIEZ1_MOUSE] Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology.[1] [2] [3] [4] [5]

References

  1. ↑ Coste B, Mathur J, Schmidt M, Earley TJ, Ranade S, Petrus MJ, Dubin AE, Patapoutian A. Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels. Science. 2010 Oct 1;330(6000):55-60. doi: 10.1126/science.1193270. Epub 2010 Sep , 2. PMID:20813920 doi:http://dx.doi.org/10.1126/science.1193270
  2. ↑ Coste B, Xiao B, Santos JS, Syeda R, Grandl J, Spencer KS, Kim SE, Schmidt M, Mathur J, Dubin AE, Montal M, Patapoutian A. Piezo proteins are pore-forming subunits of mechanically activated channels. Nature. 2012 Feb 19;483(7388):176-81. doi: 10.1038/nature10812. PMID:22343900 doi:http://dx.doi.org/10.1038/nature10812
  3. ↑ Peyronnet R, Martins JR, Duprat F, Demolombe S, Arhatte M, Jodar M, Tauc M, Duranton C, Paulais M, Teulon J, Honore E, Patel A. Piezo1-dependent stretch-activated channels are inhibited by Polycystin-2 in renal tubular epithelial cells. EMBO Rep. 2013 Dec;14(12):1143-8. doi: 10.1038/embor.2013.170. Epub 2013 Oct 25. PMID:24157948 doi:http://dx.doi.org/10.1038/embor.2013.170
  4. ↑ Ranade SS, Qiu Z, Woo SH, Hur SS, Murthy SE, Cahalan SM, Xu J, Mathur J, Bandell M, Coste B, Li YS, Chien S, Patapoutian A. Piezo1, a mechanically activated ion channel, is required for vascular development in mice. Proc Natl Acad Sci U S A. 2014 Jul 15;111(28):10347-52. doi:, 10.1073/pnas.1409233111. Epub 2014 Jun 23. PMID:24958852 doi:http://dx.doi.org/10.1073/pnas.1409233111
  5. ↑ Li J, Hou B, Tumova S, Muraki K, Bruns A, Ludlow MJ, Sedo A, Hyman AJ, McKeown L, Young RS, Yuldasheva NY, Majeed Y, Wilson LA, Rode B, Bailey MA, Kim HR, Fu Z, Carter DA, Bilton J, Imrie H, Ajuh P, Dear TN, Cubbon RM, Kearney MT, Prasad KR, Evans PC, Ainscough JF, Beech DJ. Piezo1 integration of vascular architecture with physiological force. Nature. 2014 Nov 13;515(7526):279-82. doi: 10.1038/nature13701. Epub 2014 Aug 10. PMID:25119035 doi:http://dx.doi.org/10.1038/nature13701

7wlu, resolution 6.81Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=7wlu&oldid=3626462"