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PDBsum entry 1srl
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Phosphotransferase
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PDB id
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1srl
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.10.2
- non-specific protein-tyrosine kinase.
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Reaction:
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L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
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L-tyrosyl-[protein]
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+
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ATP
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=
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O-phospho-L-tyrosyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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FEBS Lett
324:87-92
(1993)
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PubMed id:
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1H and 15N assignments and secondary structure of the Src SH3 domain.
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H.Yu,
M.K.Rosen,
S.L.Schreiber.
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ABSTRACT
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The 1H and 15N sequential assignments of the Src SH3 domain have been determined
through a combination of 2D and 3D Nuclear Magnetic Resonance (NMR) methods. The
secondary structure of the protein has been identified based on long-range NOE
patterns. The SH3 domain of Src consists largely of six beta-strands that form
two anti-parallel beta-sheets.
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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.Zhao,
Y.Zhang,
S.S.Ithychanda,
Y.Tu,
K.Chen,
J.Qin,
and
C.Wu
(2009).
Migfilin interacts with Src and contributes to cell-matrix adhesion-mediated survival signaling.
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J Biol Chem,
284,
34308-34320.
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Z.Zhuang,
A.I.Jewett,
P.Soto,
and
J.E.Shea
(2009).
The effect of surface tethering on the folding of the src-SH3 protein domain.
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Phys Biol,
6,
15004.
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A.Fernández,
J.Chen,
and
A.Crespo
(2007).
Solvent-exposed backbone loosens the hydration shell of soluble folded proteins.
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J Chem Phys,
126,
245103.
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A.Pintar,
and
S.Pongor
(2005).
The "first in-last out" hypothesis on protein folding revisited.
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Proteins,
60,
584-590.
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D.Wildes,
and
S.Marqusee
(2005).
Hydrogen exchange and ligand binding: ligand-dependent and ligand-independent protection in the Src SH3 domain.
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Protein Sci,
14,
81-88.
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K.Ikeda,
O.V.Galzitskaya,
H.Nakamura,
and
J.Higo
(2003).
beta-Hairpins, alpha-helices, and the intermediates among the secondary structures in the energy landscape of a peptide from a distal beta-hairpin of SH3 domain.
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J Comput Chem,
24,
310-318.
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R.Abseher,
and
M.Nilges
(2002).
Protein folding in mode space: a collective coordinate approach to structure prediction.
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Proteins,
49,
365-377.
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R.Li,
and
C.Woodward
(1999).
The hydrogen exchange core and protein folding.
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Protein Sci,
8,
1571-1590.
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V.P.Grantcharova,
D.S.Riddle,
J.V.Santiago,
and
D.Baker
(1998).
Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain.
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Nat Struct Biol,
5,
714-720.
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J.R.Engen,
T.E.Smithgall,
W.H.Gmeiner,
and
D.L.Smith
(1997).
Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry.
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Biochemistry,
36,
14384-14391.
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M.Thelen,
and
S.A.Didichenko
(1997).
G-protein coupled receptor-mediated activation of PI 3-kinase in neutrophils.
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Ann N Y Acad Sci,
832,
368-382.
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M.T.Pisabarro,
and
L.Serrano
(1996).
Rational design of specific high-affinity peptide ligands for the Abl-SH3 domain.
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Biochemistry,
35,
10634-10640.
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D.Kohda,
H.Terasawa,
S.Ichikawa,
K.Ogura,
H.Hatanaka,
V.Mandiyan,
A.Ullrich,
J.Schlessinger,
and
F.Inagaki
(1994).
Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2.
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Structure,
2,
1029-1040.
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PDB codes:
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M.T.Pisabarro,
A.R.Ortiz,
L.Serrano,
and
R.C.Wade
(1994).
Homology modeling of the Abl-SH3 domain.
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Proteins,
20,
203-215.
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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
codes are
shown on the right.
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Links
