About: Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin     Goto   Sponge   NotDistinct   Permalink

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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. (en)
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 (en)
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 (en)
skos:notation
  • RIV/00216224:14310/05:00039944!RIV10-MSM-14310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM0021622415)
http://linked.open...iv/cisloPeriodika
  • 10
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 511288
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/05:00039944
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Actin binding domain; vimentin; plectin (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • AT - Rakouská republika
http://linked.open...ontrolniKodProRIV
  • [1173CEB2484A]
http://linked.open...i/riv/nazevZdroje
  • 1873-84
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 271
http://linked.open...iv/tvurceVysledku
  • Janda, Lubomír
  • Wiche, Gerhard
  • Urbániková, Lubica
  • Košťan, Július
  • Ševčík, Jozef
http://linked.open...n/vavai/riv/zamer
issn
  • 0014-2956
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
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