%0 Journal Article
%A Thielmann, Y.
%A Weiergräber, O.H.
%A Mohrlüder, J.
%A Willbold, D.
%T Structural framework of the GABARAP-calreticulin interface - implications for substrate binding to endoplasmic reticulum chaperones
%J The FEBS journal
%V 276
%@ 1742-464X
%C Oxford [u.a.]
%I Wiley-Blackwell
%M PreJuSER-5170
%P 1140 - 1152
%D 2009
%Z The authors wish to thank Olga Dietz for excellent technical assistance. O. H. WeiergrAber is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the ESRF staff at beamline ID14-1 is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft (DFG) to D. Willbold (Wi1472/5).
%X The 4-aminobutyrate type A receptor-associated protein (GABARAP) is a versatile adaptor protein that plays an important role in intracellular vesicle trafficking, particularly in neuronal cells. We have investigated the structural determinants underlying the interaction of GABARAP with calreticulin using spectroscopic and crystallographic techniques. Specifically, we present the crystal structure of GABARAP in complex with its major binding epitope on the chaperone. Molecular modeling of a complex containing full-length calreticulin suggests a novel mode of substrate interaction, which may have functional implications for the calreticulin/calnexin family in general.
%K Adaptor Proteins, Signal Transducing: chemistry
%K Adaptor Proteins, Signal Transducing: metabolism
%K Calreticulin: chemistry
%K Calreticulin: metabolism
%K Endoplasmic Reticulum: metabolism
%K Humans
%K Microtubule-Associated Proteins: chemistry
%K Microtubule-Associated Proteins: metabolism
%K Models, Molecular
%K Molecular Chaperones: chemistry
%K Molecular Chaperones: metabolism
%K Protein Binding
%K Substrate Specificity
%K Adaptor Proteins, Signal Transducing (NLM Chemicals)
%K Calreticulin (NLM Chemicals)
%K GABARAP protein, human (NLM Chemicals)
%K Microtubule-Associated Proteins (NLM Chemicals)
%K Molecular Chaperones (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:19154346
%U <Go to ISI:>//WOS:000262666900022
%R 10.1111/j.1742-4658.2008.06857.x
%U https://juser.fz-juelich.de/record/5170