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PDBsum entry 3dow
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Protein transport
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PDB id
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3dow
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Protein transport
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Title:
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Complex structure of gaba type a receptor associated protein and its binding epitope on calreticulin
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Structure:
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Gamma-aminobutyric acid receptor-associated protein. Chain: a. Synonym: gaba(a) receptor-associated protein, mm46. Engineered: yes. Crt peptide. Chain: b. Synonym: calreticulin, crp55, calregulin, hacbp, erp60, grp60. Engineered: yes
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Source:
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Homo sapiens. Organism_taxid: 9606. Gene: gabarap, flc3b. Expressed in: escherichia coli. Synthetic: yes. Other_details: synthetic peptide containing amino acids 195-205 of mature calreticulin, calr_human, uniprot entry p27797
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Resolution:
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2.30Å
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R-factor:
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0.233
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R-free:
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0.270
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Authors:
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Y.Thielmann,O.H.Weiergraeber,D.Willbold
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Key ref:
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Y.Thielmann
et al.
(2009).
Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones.
Febs J,
276,
1140-1152.
PubMed id:
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Date:
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07-Jul-08
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Release date:
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24-Feb-09
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PROCHECK
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Headers
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References
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O95166
(GBRAP_HUMAN) -
Gamma-aminobutyric acid receptor-associated protein from Homo sapiens
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Seq:
Struc:
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117 a.a.
119 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Febs J
276:1140-1152
(2009)
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PubMed id:
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Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones.
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Y.Thielmann,
O.H.Weiergräber,
J.Mohrlüder,
D.Willbold.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.M.Winget,
and
T.Mayor
(2010).
The diversity of ubiquitin recognition: hot spots and varied specificity.
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Mol Cell,
38,
627-635.
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P.Ma,
J.Mohrlüder,
M.Schwarten,
M.Stoldt,
S.K.Singh,
R.Hartmann,
V.Pacheco,
and
D.Willbold
(2010).
Preparation of a functional GABARAP-lipid conjugate in nanodiscs and its investigation by solution NMR spectroscopy.
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Chembiochem,
11,
1967-1970.
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S.Ling,
A.Cheng,
P.Pumpens,
M.Michalak,
and
J.Holoshitz
(2010).
Identification of the rheumatoid arthritis shared epitope binding site on calreticulin.
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PLoS One,
5,
e11703.
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V.Pacheco,
P.Ma,
Y.Thielmann,
R.Hartmann,
O.H.Weiergräber,
J.Mohrlüder,
and
D.Willbold
(2010).
Assessment of GABARAP self-association by its diffusion properties.
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J Biomol NMR,
48,
49-58.
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J.Mohrlüder,
M.Schwarten,
and
D.Willbold
(2009).
Structure and potential function of gamma-aminobutyrate type A receptor-associated protein.
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FEBS J,
276,
4989-5005.
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Y.Thielmann,
O.H.Weiergräber,
J.Mohrlüder,
and
D.Willbold
(2009).
Structural characterization of GABARAP-ligand interactions.
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Mol Biosyst,
5,
575-579.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
