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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F05%3A00039944%21RIV10-MSM-14310___
rdf:type
skos:Concept n16:Vysledek
dcterms:description
Plectin, a large and widely expressed cytolinker protein, is composed of several subdomains that harbor binding sites for a variety of different interaction partners. A canonical actin-binding domain (ABD) comprising two calponin homology domains (CH1 and CH2) is located in proximity to its amino terminus. However, the ABD of plectin is unique among actin-binding proteins as it is expressed in the form of distinct, plectin isoform-specific versions. We have determined the three-dimensional structure of two distinct crystalline forms of one of its ABD versions (pleABD/2alpha) from mouse, to a resolution of 1.95 and 2.0 A. Comparison of pleABD/2alpha with the ABDs of fimbrin and utrophin revealed structural similarity between plectin and fimbrin, although the proteins share only low sequence identity. In fact, pleABD/2alpha has been found to have the same compact fold as the human plectin ABD and the fimbrin ABD, differing from the open conformation described for the ABDs of utrophin and dystrophin. Plectin, a large and widely expressed cytolinker protein, is composed of several subdomains that harbor binding sites for a variety of different interaction partners. A canonical actin-binding domain (ABD) comprising two calponin homology domains (CH1 and CH2) is located in proximity to its amino terminus. However, the ABD of plectin is unique among actin-binding proteins as it is expressed in the form of distinct, plectin isoform-specific versions. We have determined the three-dimensional structure of two distinct crystalline forms of one of its ABD versions (pleABD/2alpha) from mouse, to a resolution of 1.95 and 2.0 A. Comparison of pleABD/2alpha with the ABDs of fimbrin and utrophin revealed structural similarity between plectin and fimbrin, although the proteins share only low sequence identity. In fact, pleABD/2alpha has been found to have the same compact fold as the human plectin ABD and the fimbrin ABD, differing from the open conformation described for the ABDs of utrophin and dystrophin.
dcterms:title
Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
skos:prefLabel
Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
skos:notation
RIV/00216224:14310/05:00039944!RIV10-MSM-14310___
n4:aktivita
n8:Z
n4:aktivity
Z(MSM0021622415)
n4:cisloPeriodika
10
n4:dodaniDat
n10:2010
n4:domaciTvurceVysledku
n5:2503700 n5:1645102 n5:6817734
n4:druhVysledku
n13:J
n4:duvernostUdaju
n7:S
n4:entitaPredkladatele
n14:predkladatel
n4:idSjednocenehoVysledku
511288
n4:idVysledku
RIV/00216224:14310/05:00039944
n4:jazykVysledku
n17:eng
n4:klicovaSlova
Actin binding domain; vimentin; plectin
n4:klicoveSlovo
n6:Actin%20binding%20domain n6:vimentin n6:plectin
n4:kodStatuVydavatele
AT - Rakouská republika
n4:kontrolniKodProRIV
[1173CEB2484A]
n4:nazevZdroje
1873-84
n4:obor
n15:CE
n4:pocetDomacichTvurcuVysledku
3
n4:pocetTvurcuVysledku
5
n4:rokUplatneniVysledku
n10:2005
n4:svazekPeriodika
271
n4:tvurceVysledku
Wiche, Gerhard Janda, Lubomír Ševčík, Jozef Urbániková, Lubica Košťan, Július
n4:zamer
n11:MSM0021622415
s:issn
0014-2956
s:numberOfPages
2004
n18:organizacniJednotka
14310