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PDBsum entry 4icz
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References listed in PDB file
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Key reference
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Title
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Her2 1221/1222 phosphorylation regulated by ptpn9
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Authors
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Y.F.Xu,
H.M.Wang,
C.H.Liu,
X.Yu,
J.P.Sun.
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Ref.
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TO BE PUBLISHED ...
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Secondary reference #1
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Title
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Large-Scale structural analysis of the classical human protein tyrosine phosphatome.
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Authors
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A.J.Barr,
E.Ugochukwu,
W.H.Lee,
O.N.King,
P.Filippakopoulos,
I.Alfano,
P.Savitsky,
N.A.Burgess-Brown,
S.Müller,
S.Knapp.
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Ref.
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Cell, 2009,
136,
352-363.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. Novel Conformations and Movement of the Catalytic
(WPD) Loop
(A) WPD loop conformations are shown by a PTP
representative of each state: closed (blue, PTP1B, PDB: 1SUG);
open (yellow, PTP1B, PDB: 2HNP); and atypical (magenta, GLEPP1,
PDB: 2GJT; STEP, PDB: 2BIJ; Lyp, PDB: 2P6X). The intermediate
WPD loop conformation of PCPTP1 (PDB: 2A8B) is not shown for
clarity. Other PTP structures are shown with a thin transparent
line tracing the backbone and are colored according to
conformation.
(B) Superimposition of the structure of
STEP-C/S in complex with pY (PDB: 2CJZ; gray) and the apo STEP
(PDB: 2BIJ; light green) showing that the WPD loop conformation
does not change on substrate binding (pTyr, orange). The
catalytic water molecule (Wa) corresponding to that found in
closed structures is shown.
(C) Superimposition of the
structure of STEP-C/S in complex with pY (PDB: 2CJZ; green) and
PTP1B with the insulin receptor peptide (PDB: 1G1H; red). The
conserved water molecule found in closed structures is shown:
PTP1B (1SUG, yellow); GLEPP1 (2G59, orange); HePTP (2A3K,
black), DEP1 (2NZ6, magenta). The arrow indicates the position
of the displaced water molecule in STEP-C/S structure.
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Figure 4.
Figure 4. Secondary Substrate-Binding Pockets
(A) Two
extreme conformations of the second-site loop are shown (orange)
from RPTPγ (extended helix) and HEPTP (closed in conformation).
The catalytic cysteine is shown in a space-filling CPK
representation, and loops are colored as follows: WPD (magenta),
β5/β6 loop (green), and gateway (red). The dually pTyr
phosphorylated insulin receptor peptide (from PDB: 1G1H) is
shown superimposed (for reference only) to indicate the position
of the secondary substrate-binding pocket. The positions of
Arg24 and gateway residues Met258 and Gly259 of PTP1B are shown
in an enlarged view.
(B) Surface topology and electrostatic
charge for the active site (pY), gateway region, and secondary
pocket (2pY) are shown for each of the five categories with the
dually pTyr phosphorylated insulin receptor peptide
superimposed.
(C) Representative second-site loop
conformations are shown for each category (see also Supplemental
Data). Category I: SHP2, BDP1, LYP; Category II: IA2, IA2β;
Category III: LAR, RPTPσ; Category IV: PTPH1, MEG1, PTPD2,
CD45; Category V: STEP, HEPTP, PCPTP1.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by Cell Press
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