Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.
about
The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants.Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry.Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface.
P2860
Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.
description
2017 nî lūn-bûn
@nan
2017 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2017 թվականի մարտին հրատարակված գիտական հոդված
@hy
2017年の論文
@ja
2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
name
Structural model of dodecameri ...... ecamer and chaperone activity.
@ast
Structural model of dodecameri ...... ecamer and chaperone activity.
@en
type
label
Structural model of dodecameri ...... ecamer and chaperone activity.
@ast
Structural model of dodecameri ...... ecamer and chaperone activity.
@en
prefLabel
Structural model of dodecameri ...... ecamer and chaperone activity.
@ast
Structural model of dodecameri ...... ecamer and chaperone activity.
@en
P2093
P2860
P356
P1476
Structural model of dodecameri ...... decamer and chaperone activity
@en
P2093
Cecilia Emanuelsson
Christopher A G Söderberg
Gudrun Rutsdottir
Hans Hebert
Johan Härmark
Michal Respondek
Morten I Rasmussen
Peter Højrup
Philip J B Koeck
Sven Wernersson
P2860
P304
P356
10.1074/JBC.M116.766816
P407
P50
P577
2017-03-21T00:00:00Z