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PDBsum entry 2kbt
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Signaling protein
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PDB id
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2kbt
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Contents |
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* Residue conservation analysis
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PDB id:
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Signaling protein
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Title:
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Attachment of an nmr-invisible solubility enhancement tag (inset) using a sortase-mediated protein ligation method
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Structure:
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Proto-oncogene vav,immunoglobulin g-binding protein g. Chain: a. Fragment: sh3 2 domain of proto-oncogene vav,unp residues 228-282 of immunoglobulin g-binding protein g. Synonym: p95vav,igg-binding protein g. Engineered: yes. Other_details: a solubility-enhancement tag (set) gb1, domain of immunoglobulin g-binding protein g (invisible gb1 tag), is non- labeled and attached to thE C-terminal of 13c/15n-labeled vav sh3
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Source:
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Mus musculus, streptococcus sp. 'Group g'. House mouse. Organism_taxid: 10090, 1320. Gene: vav1, vav, spg. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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H.Kumeta,Y.Kobashigawa,K.Ogura,F.Inagaki
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Key ref:
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Y.Kobashigawa
et al.
(2009).
Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method.
J Biomol Nmr,
43,
145-150.
PubMed id:
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Date:
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07-Dec-08
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Release date:
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03-Feb-09
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PROCHECK
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Headers
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References
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J Biomol Nmr
43:145-150
(2009)
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PubMed id:
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Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method.
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Y.Kobashigawa,
H.Kumeta,
K.Ogura,
F.Inagaki.
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ABSTRACT
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Sample solubility is essential for structural studies of proteins by solution
NMR. Attachment of a solubility enhancement tag, such as GB1, MBP and
thioredoxin, to a target protein has been used for this purpose. However, signal
overlap of the tag with the target protein often made the spectral analysis
difficult. Here we report a sortase-mediated protein ligation method to
eliminate NMR signals arising from the tag by preparing the isotopically labeled
target protein attached with the non-labeled GB1 tag at the C-terminus.
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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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M.Yamaguchi,
K.Matoba,
R.Sawada,
Y.Fujioka,
H.Nakatogawa,
H.Yamamoto,
Y.Kobashigawa,
H.Hoshida,
R.Akada,
Y.Ohsumi,
N.N.Noda,
and
F.Inagaki
(2012).
Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7.
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Nat Struct Mol Biol,
19,
1250-1256.
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C.Dominguez,
M.Schubert,
O.Duss,
S.Ravindranathan,
and
F.H.Allain
(2011).
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
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Prog Nucl Magn Reson Spectrosc,
58,
1.
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M.A.Refaei,
A.Combs,
D.J.Kojetin,
J.Cavanagh,
C.Caperelli,
M.Rance,
J.Sapitro,
and
P.Tsang
(2011).
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy.
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J Biomol NMR,
49,
3-7.
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K.Hayashi,
and
C.Kojima
(2010).
Efficient protein production method for NMR using soluble protein tags with cold shock expression vector.
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J Biomol NMR,
48,
147-155.
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K.W.Clancy,
J.A.Melvin,
and
D.G.McCafferty
(2010).
Sortase transpeptidases: insights into mechanism, substrate specificity, and inhibition.
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Biopolymers,
94,
385-396.
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L.Skrisovska,
M.Schubert,
and
F.H.Allain
(2010).
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins.
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J Biomol NMR,
46,
51-65.
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P.Zhou,
and
G.Wagner
(2010).
Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.
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J Biomol NMR,
46,
23-31.
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Y.Kobashigawa,
H.Kumeta,
D.Kanoh,
and
F.Inagaki
(2009).
The NMR structure of the TC10- and Cdc42-interacting domain of CIP4.
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J Biomol NMR,
44,
113-118.
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PDB code:
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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