SASDAS6: Plectin, fragment of the plakin domain encompassing the spectrin ...

Basic information

• Entry: Database: SASBDB / ID: SASDAS6

Sample

Plectin, fragment of the plakin domain encompassing the spectrin repeats SR3-SR4-SR5 and the SH3

• Plectin (protein), Homo sapiens

Function / homology

Function:

protein-containing complex organization / actomyosin contractile ring assembly actin filament organization / skeletal myofibril assembly / tight junction organization / Type I hemidesmosome assembly / hemidesmosome assembly / hemidesmosome / leukocyte migration involved in immune response / intermediate filament organization / : / regulation of vascular permeability / intermediate filament cytoskeleton organization / dystroglycan binding / cellular response to hydrostatic pressure / fibroblast migration / T cell chemotaxis / costamere / cellular response to fluid shear stress / peripheral nervous system myelin maintenance / cardiac muscle cell development / myoblast differentiation / adherens junction organization / intermediate filament / intermediate filament cytoskeleton / nucleus organization / response to food / structural constituent of muscle / ankyrin binding / Assembly of collagen fibrils and other multimeric structures / sarcomere organization / keratinocyte development / transmission of nerve impulse / brush border / sarcoplasm / Caspase-mediated cleavage of cytoskeletal proteins / establishment of skin barrier / skeletal muscle fiber development / respiratory electron transport chain / mitochondrion organization / multicellular organism growth / sarcolemma / wound healing / cell morphogenesis / protein localization / structural constituent of cytoskeleton / Z disc / cellular response to mechanical stimulus / : / actin filament binding / myelin sheath / gene expression / mitochondrial outer membrane / cadherin binding / axon / focal adhesion / dendrite / perinuclear region of cytoplasm / RNA binding / extracellular exosome / plasma membrane / cytosol / cytoplasm

Domain/homology:

: / Spectrin-like repeat / Spectrin repeat / Spectrin-like repeat / Desmoplakin, spectrin-like domain / Spectrin like domain / Plectin repeat / Plectin repeat / Plakin repeat superfamily / Desmoplakin, SH3 domain / SH3 domain / Plectin repeat / Plakin / Spectrin/alpha-actinin / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Spectrin repeats / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Plectin/S10, N-terminal / Plectin/S10 domain / Src homology 3 (SH3) domain profile. / SH3 domain / Winged helix-like DNA-binding domain superfamily

Component:

Plectin

• Biological species: Homo sapiens (human)
• Citation: Journal: J Biol Chem / Year: 2011; Title: The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat.; Authors: Esther Ortega / Rubén M Buey / Arnoud Sonnenberg / José M de Pereda / ; Abstract: Plectin belongs to the plakin family of cytoskeletal crosslinkers, which is part of the spectrin superfamily. Plakins contain an N-terminal conserved region, the plakin domain, which is formed by an array of spectrin repeats (SR) and a Src-homology 3 (SH3), and harbors binding sites for junctional proteins. We have combined x-ray crystallography and small angle x-ray scattering (SAXS) to elucidate the structure of the central region of the plakin domain of plectin, which corresponds to the SR3, SR4, SR5, and SH3 domains. The crystal structures of the SR3-SR4 and SR4-SR5-SH3 fragments were determined to 2.2 and 2.95 Å resolution, respectively. The SH3 of plectin presents major alterations as compared with canonical Pro-rich binding SH3 domains, suggesting that plectin does not recognize Pro-rich motifs. In addition, the SH3 binding site is partially occluded by an intramolecular contact with the SR4. Residues of this pseudo-binding site and the SR4/SH3 interface are conserved within the plakin family, suggesting that the structure of this part of the plectin molecule is similar to that of other plakins. We have created a model for the SR3-SR4-SR5-SH3 region, which agrees well with SAXS data in solution. The three SRs form a semi-flexible rod that is not altered by the presence of the SH3 domain, and it is similar to those found in spectrins. The flexibility of the plakin domain, in analogy with spectrins, might contribute to the role of plakins in maintaining the stability of tissues subject to mechanical stress.

Contact author

• Jose M de Pereda (USAL, La Universidad de Salamanca, Salamanca, Spain)

Models

• Model #218: ; Type: dummy / Software: DAMMIF / Radius of dummy atoms: 3.00 A / Chi-square value: 1.48328041; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Plectin, fragment of the plakin domain encompassing the spectrin repeats SR3-SR4-SR5 and the SH3; Specimen concentration: 1.20-9.60
• Buffer: Name: Sodium Phosphate / Concentration: 20.00 mM / pH: 7.5 / Composition: 150 mM NaCl, 5% glycerol, 2.5 mM DTT

Entity #132

Type: protein / Description: Plectin / Formula weight: 42.896 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: Q15149
Sequence:

ELEDSTLRYL QDLLAWVEEN QHRVDGAEWG VDLPSVEAQL GSHRGLHQSI EEFRAKIERA RSDEGQLSPA TRGAYRDCLG RLDLQYAKLL NSSKARLRSL ESLHSFVAAA TKELMWLNEK EEEEVGFDWS DRNTNMTAKK ESYSALMREL ELKEKKIKEL QNAGDRLLRE DHPARPTVES FQAALQTQWS WMLQLCCCIE AHLKENAAYF QFFSDVREAE GQLQKLQEAL RRKYSCDRSA TVTRLEDLLQ DAQDEKEQLN EYKGHLSGLA KRAKAVVQLK PRHPAHPMRG RLPLLAVCDY KQVEVTVHKG DECQLVGPAQ PSHWKVLSSS GSEAAVPSVC FLVPPPNQEA QEAVTRLEAQ HQALVTLWHQ LHVDMK

Experimental information

• Beam: Instrument name: Swiss Light Source cSAXS / City: Villigen / 国: Switzerland / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 2.15 mm
• Detector: Name: Pilatus 2M

Scan

Title: Plectin / Measurement date: Jul 24, 2009 / Cell temperature: 10 °C / Exposure time: 0.5 sec. / Number of frames: 60 / Unit: 1/nm /

	Min	Max
Q	0.1709	3.5044

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 280 /

	Min	Max
Q	0.2136	3.011
P(R) point	8	287
R	0	14.5

Result

D max: 14.5 / Type of curve: extrapolated
Comments: Use of SAXS to analyze the structure of central region of the plakin domain of plectin.

	Experimental	Porod
MW	37.7 kDa	33 kDa
Volume	-	57 nm3

	P(R)	Guinier
Forward scattering, I0	22.4	23.7
Radius of gyration, Rg	4.2 nm	4.4 nm