[English] 日本語
Yorodumi
- SASDBD4: Plakin domain fragment of Human desmoplakin (C-terminal region sp... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: SASBDB / ID: SASDBD4
SamplePlakin domain fragment of Human desmoplakin (C-terminal region spectrin repeats: SR7-SR8-SR9)
  • Plakin domain fragment of Human Desmoplakin encompassing spectrin repeats SR7-SR8-SR9 (protein), Desmoplakin, Homo sapiens
Function / homology
Function and homology information


bundle of His cell-Purkinje myocyte adhesion involved in cell communication / cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication / desmosome organization / Keratinization / protein localization to cell-cell junction / ventricular compact myocardium morphogenesis / intermediate filament organization / epithelial cell-cell adhesion / intermediate filament cytoskeleton organization / desmosome ...bundle of His cell-Purkinje myocyte adhesion involved in cell communication / cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication / desmosome organization / Keratinization / protein localization to cell-cell junction / ventricular compact myocardium morphogenesis / intermediate filament organization / epithelial cell-cell adhesion / intermediate filament cytoskeleton organization / desmosome / Formation of the cornified envelope / peptide cross-linking / fascia adherens / cornified envelope / regulation of ventricular cardiac muscle cell action potential / Apoptotic cleavage of cell adhesion proteins / adherens junction organization / RND1 GTPase cycle / RND3 GTPase cycle / intermediate filament / skin development / regulation of heart rate by cardiac conduction / ficolin-1-rich granule membrane / intercalated disc / epidermis development / keratinocyte differentiation / adherens junction / protein kinase C binding / wound healing / structural constituent of cytoskeleton / cell-cell adhesion / scaffold protein binding / basolateral plasma membrane / Neutrophil degranulation / structural molecule activity / RNA binding / extracellular exosome / nucleus / plasma membrane / cytoplasm
Similarity search - Function
Desmoplakin, spectrin-like domain / Spectrin like domain / Plectin repeat / Plectin repeat / Plakin repeat superfamily / Desmoplakin, SH3 domain / SH3 domain / Spectrin-like repeat / Plectin repeat / Plakin ...Desmoplakin, spectrin-like domain / Spectrin like domain / Plectin repeat / Plectin repeat / Plakin repeat superfamily / Desmoplakin, SH3 domain / SH3 domain / Spectrin-like repeat / Plectin repeat / Plakin / Spectrin/alpha-actinin / Spectrin repeats / Src homology 3 (SH3) domain profile. / SH3 domain
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationJournal: J Biol Chem / Year: 2016
Title: The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.
Authors: Esther Ortega / José A Manso / Rubén M Buey / Ana M Carballido / Arturo Carabias / Arnoud Sonnenberg / José M de Pereda /
Abstract: Plakins are large multi-domain proteins that interconnect cytoskeletal structures. Plectin is a prototypical plakin that tethers intermediate filaments to membrane-associated complexes. Most plakins ...Plakins are large multi-domain proteins that interconnect cytoskeletal structures. Plectin is a prototypical plakin that tethers intermediate filaments to membrane-associated complexes. Most plakins contain a plakin domain formed by up to nine spectrin repeats (SR1-SR9) and an SH3 domain. The plakin domains of plectin and other plakins harbor binding sites for junctional proteins. We have combined x-ray crystallography with small angle x-ray scattering (SAXS) to elucidate the structure of the plakin domain of plectin, extending our previous analysis of the SR1 to SR5 region. Two crystal structures of the SR5-SR6 region allowed us to characterize its uniquely wide inter-repeat conformational variability. We also report the crystal structures of the SR7-SR8 region, refined to 1.8 Å, and the SR7-SR9 at lower resolution. The SR7-SR9 region, which is conserved in all other plakin domains, forms a rigid segment stabilized by uniquely extensive inter-repeat contacts mediated by unusually long helices in SR8 and SR9. Using SAXS we show that in solution the SR3-SR6 and SR7-SR9 regions are rod-like segments and that SR3-SR9 of plectin has an extended shape with a small central kink. Other plakins, such as bullous pemphigoid antigen 1 and microtubule and actin cross-linking factor 1, are likely to have similar extended plakin domains. In contrast, desmoplakin has a two-segment structure with a central flexible hinge. The continuous versus segmented structures of the plakin domains of plectin and desmoplakin give insight into how different plakins might respond to tension and transmit mechanical signals.
Contact author
  • Jose M de Pereda (USAL, La Universidad de Salamanca, Salamanca, Spain)

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Models

Model #497
Type: dummy / Software: DAMMIF / Radius of dummy atoms: 3.50 A / Chi-square value: 1.393 / P-value: 0.415500
Search similar-shape structures of this assembly by Omokage search (details)

-
Sample

SampleName: Plakin domain fragment of Human desmoplakin (C-terminal region spectrin repeats: SR7-SR8-SR9)
Specimen concentration: 0.96-7.70
BufferName: sodium phosphate / Concentration: 20.00 mM / pH: 7.5 / Composition: 150 mM NaCl, 5% glycerol, 3 mM DTT
Entity #322Name: Desmoplakin / Type: protein
Description: Plakin domain fragment of Human Desmoplakin encompassing spectrin repeats SR7-SR8-SR9
Formula weight: 41.982 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P15924
Sequence: GSHMENDKQE TWMLMELQKI RRQIEHCEGR MTLKNLPLAD QGSSHHITVK INELKSVQND SQAIAEVLNQ LKDMLANFRG SEKYCYLQNE VFGLFQKLEN INGVTDGYLN SLCTVRALLQ AILQTEDMLK VYEARLTEEE TVCLDLDKVE AYRCGLKKIK NDLNLKKSLL ...Sequence:
GSHMENDKQE TWMLMELQKI RRQIEHCEGR MTLKNLPLAD QGSSHHITVK INELKSVQND SQAIAEVLNQ LKDMLANFRG SEKYCYLQNE VFGLFQKLEN INGVTDGYLN SLCTVRALLQ AILQTEDMLK VYEARLTEEE TVCLDLDKVE AYRCGLKKIK NDLNLKKSLL ATMKTELQKA QQIHSQTSQQ YPLYDLDLGK FGEKVTQLTD RWQRIDKQID FRLWDLEKQI KQLRNYRDNY QAFCKWLYDA KRRQDSLESM KFGDSNTVMR FLNEQKNLHS EISGKRDKSE EVQKIAELCA NSIKDYELQL ASYTSGLETL LNIPIKRTMI QSPSGVILQE AADVHARYIE LLTRSGDYYR

-
Experimental information

BeamInstrument name: PETRA III P12 / City: Hamburg / : Germany / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: Plakin domain fragment of Human desmoplakin / Measurement date: Sep 25, 2015 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 30 / Unit: 1/nm /
MinMax
Q0.0886 4.8124
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1103 /
MinMax
Q0.088642 3.00166
P(R) point1 1103
R0 17.5
Result
D max: 17.5 / Type of curve: extrapolated /
ExperimentalPorod
MW44.9 kDa43.4 kDa
Volume-69.4 nm3

P(R)Guinier
Forward scattering, I010110 9950
Radius of gyration, Rg4.72 nm4.41 nm

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more