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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Human PIEZO1-R2456H_MDFIC | |||||||||
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![]() | Human PIEZO1 / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() mechanosensitive monoatomic cation channel activity / positive regulation of viral transcription / cuticular plate / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / positive regulation of integrin activation / mechanosensitive monoatomic ion channel activity / Tat protein binding / stereocilium / regulation of Wnt signaling pathway ...mechanosensitive monoatomic cation channel activity / positive regulation of viral transcription / cuticular plate / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / positive regulation of integrin activation / mechanosensitive monoatomic ion channel activity / Tat protein binding / stereocilium / regulation of Wnt signaling pathway / regulation of JNK cascade / Mechanical load activates signaling by PIEZO1 and integrins in osteocytes / negative regulation of protein import into nucleus / positive regulation of myotube differentiation / lamellipodium membrane / monoatomic cation transport / monoatomic cation channel activity / endoplasmic reticulum-Golgi intermediate compartment membrane / cyclin binding / Turbulent (oscillatory, disturbed) flow shear stress activates signaling by PIEZO1 and integrins in endothelial cells / regulation of membrane potential / cellular response to mechanical stimulus / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / DNA-binding transcription factor binding / negative regulation of DNA-templated transcription / endoplasmic reticulum membrane / positive regulation of DNA-templated transcription / nucleolus / endoplasmic reticulum / extracellular region / nucleus / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.5 Å | |||||||||
![]() | Zhang MF | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of human PIEZO1 and its slow inactivating channelopathy mutants. Authors: Shan Y / Guo X / Zhang M / Chen M / Li Y / Zhang MF / Pei D | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.3 GB | ![]() | |
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Header (meta data) | ![]() ![]() | 16 KB 16 KB | Display Display | ![]() |
Images | ![]() | 60 KB | ||
Filedesc metadata | ![]() | 6.8 KB | ||
Others | ![]() ![]() | 1.3 GB 1.3 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8yfgMC ![]() 8yezC ![]() 8yfcC ![]() 8zu3C ![]() 8zu8C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.57 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_39223_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_39223_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : human PIEZO1
Entire | Name: human PIEZO1 |
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Components |
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-Supramolecule #1: human PIEZO1
Supramolecule | Name: human PIEZO1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Piezo-type mechanosensitive ion channel component 1
Macromolecule | Name: Piezo-type mechanosensitive ion channel component 1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 287.075 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MEPHVLGAVL YWLLLPCALL AACLLRFSGL SLVYLLFLLL LPWFPGPTRC GLQGHTGRLL RALLGLSLLF LVAHLALQIC LHIVPRLDQ LLGPSCSRWE TLSRHIGVTR LDLKDIPNAI RLVAPDLGIL VVSSVCLGIC GRLARNTRQS PHPRELDDDE R DVDASPTA ...String: MEPHVLGAVL YWLLLPCALL AACLLRFSGL SLVYLLFLLL LPWFPGPTRC GLQGHTGRLL RALLGLSLLF LVAHLALQIC LHIVPRLDQ LLGPSCSRWE TLSRHIGVTR LDLKDIPNAI RLVAPDLGIL VVSSVCLGIC GRLARNTRQS PHPRELDDDE R DVDASPTA GLQEAATLAP TRRSRLAARF RVTAHWLLVA AGRVLAVTLL ALAGIAHPSA LSSVYLLLFL ALCTWWACHF PI STRGFSR LCVAVGCFGA GHLICLYCYQ MPLAQALLPP AGIWARVLGL KDFVGPTNCS SPHALVLNTG LDWPVYASPG VLL LLCYAT ASLRKLRAYR PSGQRKEAAK GYEARELELA ELDQWPQERE SDQHVVPTAP DTEADNCIVH ELTGQSSVLR RPVR PKRAE PREASPLHSL GHLIMDQSYV CALIAMMVWS ITYHSWLTFV LLLWACLIWT VRSRHQLAML CSPCILLYGM TLCCL RYVW AMDLRPELPT TLGPVSLRQL GLEHTRYPCL DLGAMLLYTL TFWLLLRQFV KEKLLKWAES PAALTEVTVA DTEPTR TQT LLQSLGELVK GVYAKYWIYV CAGMFIVVSF AGRLVVYKIV YMFLFLLCLT LFQVYYSLWR KLLKAFWWLV VAYTMLV LI AVYTFQFQDF PAYWRNLTGF TDEQLGDLGL EQFSVSELFS SILVPGFFLL ACILQLHYFH RPFMQLTDME HVSLPGTR L PRWAHRQDAV SGTPLLREEQ QEHQQQQQEE EEEEEDSRDE GLGVATPHQA TQVPEGAAKW GLVAERLLEL AAGFSDVLS RVQVFLRRLL ELHVFKLVAL YTVWVALKEV SVMNLLLVVL WAFALPYPRF RPMASCLSTV WTCVIIVCKM LYQLKVVNPQ EYSSNCTEP FPNSTNLLPT EISQSLLYRG PVDPANWFGV RKGFPNLGYI QNHLQVLLLL VFEAIVYRRQ EHYRRQHQLA P LPAQAVFA SGTRQQLDQD LLGCLKYFIN FFFYKFGLEI CFLMAVNVIG QRMNFLVTLH GCWLVAILTR RHRQAIARLW PN YCLFLAL FLLYQYLLCL GMPPALCIDY PWRWSRAVPM NSALIKWLYL PDFFRAPNST NLISDFLLLL CASQQWQVFS AER TEEWQR MAGVNTDRLE PLRGEPNPVP NFIHCRSYLD MLKVAVFRYL FWLVLVVVFV TGATRISIFG LGYLLACFYL LLFG TALLQ RDTRARLVLW DCLILYNVTV IISKNMLSLL ACVFVEQMQT GFCWVIQLFS LVCTVKGYYD PKEMMDRDQD CLLPV EEAG IIWDSVCFFF LLLQRRVFLS HYYLHVRADL QATALLASRG FALYNAANLK SIDFHRRIEE KSLAQLKRQM ERIRAK QEK HRQGRVDRSR PQDTLGPKDP GLEPGPDSPG GSSPPRRQWW RPWLDHATVI HSGDYFLFES DSEEEEEAVP EDPRPSA QS AFQLAYQAWV TNAQAVLRRR QQEQEQARQE QAGQLPTGGG PSQEVEPAEG PEEAAAGRSH VVQRVLSTAQ FLWMLGQA L VDELTRWLQE FTRHHGTMSD VLRAERYLLT QELLQGGEVH RGVLDQLYTS QAEATLPGPT EAPNAPSTVS SGLGAEEPL SSMTDDMGSP LSTGYHTRSG SEEAVTDPGE REAGASLYQG LMRTASELLL DRRLRIPELE EAELFAEGQG RALRLLRAVY QCVAAHSEL LCYFIIILNH MVTASAGSLV LPVLVFLWAM LSIPRPSKRF WMTAIVFTEI AVVVKYLFQF GFFPWNSHVV L RRYENKPY FPPRILGLEK TDGYIKYDLV QLMALFFHRS QLLCYGLWDH EEDSPSKEHD KSGEEEQGAE EGPGVPAATT ED HIQVEAR VGPTDGTPEP QVELRPRDTR RISLRFRRRK KEGPARKGAA AIEAEDREEE EGEEEKEAPT GREKRPSRSG GRV RAAGRR LQGFCLSLAQ GTYRPLRRFF HDILHTKYRA ATDVYALMFL ADVVDFIIII FGFWAFGKHS AATDITSSLS DDQV PEAFL VMLLIQFSTM VVDRALYLRK TVLGKLAFQV ALVLAIHLWM FFILPAVTER MFNQNVVAQL WYFVKCIYFA LSAYQ IRCG YPTRILGNFL TKKYNHLNLF LFQGFRLVPF LVELRAVMDW VWTDTTLSLS SWMCVEDIYA NIFIIKCSRE TEKKYP QPK GQKKKKIVKY GMGGLIILFL IAIIWFPLLF MSLVRSVVGV VNQPIDVTVT LKLGGYEPLF TMSAQQPSII PFTAQAY EE LSRQFDPQPL AMQFISQYSP EDIVTAQIEG SSGALWRISP PSRAQMKREL YNGTADITLR FTWNFQRDLA KGGTVEYA N EKHMLALAPN STARRQLASL LEGTSDQSVV IPNLFPKYIR APNGPEANPV KQLQPNEEAD YLGVRIQLRR EQGAGATGF LEWWVIELQE CRTDCNLLPM VIFSDKVSPP SLGFLAGYGI MGLYVSIVLV IGKFVHGFFS EISHSIMFEE LPCVDRILKL CQDIFLVRE TRELELEEEL YAKLIFLYRS PETMIKWTRE KE UniProtKB: Piezo-type mechanosensitive ion channel component 1 |
-Macromolecule #2: MyoD family inhibitor domain-containing protein
Macromolecule | Name: MyoD family inhibitor domain-containing protein / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 25.814113 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MSGAGEALAP GPVGPQRVAE AGGGQLGSTA QGKCDKDNTE KDITQATNSH FTHGEMQDQS IWGNPSDGEL IRTQPQRLPQ LQTSAQVPS GEEIGKIKNG HTGLSNGNGI HHGAKHGSAD NRKLSAPVSQ KMHRKIQSSL SVNSDISKKS KVNAVFSQKT G SSPEDCCV ...String: MSGAGEALAP GPVGPQRVAE AGGGQLGSTA QGKCDKDNTE KDITQATNSH FTHGEMQDQS IWGNPSDGEL IRTQPQRLPQ LQTSAQVPS GEEIGKIKNG HTGLSNGNGI HHGAKHGSAD NRKLSAPVSQ KMHRKIQSSL SVNSDISKKS KVNAVFSQKT G SSPEDCCV HCILACLFCE FLTLCNIVLG QASCGICTSE ACCCCCGDEM GDDCNCPCDM DCGIMDACCE SSDCLEICME CC GICFPS UniProtKB: MyoD family inhibitor domain-containing protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TECNAI 10 |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 16739 |
Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: NOT APPLICABLE |