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PDBsum entry 1z8d
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References listed in PDB file
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Key reference
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Title
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The crystal structure of human muscle glycogen phosphorylase a with bound glucose and AMP: an intermediate conformation with t-State and r-State features.
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Authors
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C.M.Lukacs,
N.G.Oikonomakos,
R.L.Crowther,
L.N.Hong,
R.U.Kammlott,
W.Levin,
S.Li,
C.M.Liu,
D.Lucas-Mcgady,
S.Pietranico,
L.Reik.
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Ref.
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Proteins, 2006,
63,
1123-1126.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 1.
Figure 1. (a) The overall fold of human muscle glycogen
phosphorylase a. Because there was one molecule in the
asymmetric unit, the active dimer was generated using a symmetry
related molecule. Glucose, AMP, PLP, P-Ser 14, and adenine are
shown and labeled. The positions of amino acids that differ
between the human and rabbit muscle enzyme are shown in the blue
monomer as yellow spheres. Figures were made with MOLSCRIPT[35]
and Raster3D.[36] (b) Stereoview of the interactions between
human muscle GPa and AMP. These interactions include extensive
water-mediated contacts from the phosphate groups, several
direct hydrogen bonds between the adenine and the AMP binding
loop, and one hydrogen bond between the ribose and the cap
region of the dimeric molecule. Van der Waals contacts from the
adenine include an edge-to-face interaction with Phe 316 and a
stacking interaction with Tyr 75. 2Fo-Fc density for the AMP is
shown at 1  contour
level. (c) Superposition of human muscle glycogen phosphorylase
a (yellow) with human liver GPa with AMP bound (1FA9[6]) in
orange and rabbit muscle GPb with AMP bound (7GPB[27]) in cyan,
highlighting the difference in the allosteric site loop
surrounding the AMP. Phe 316 is shown in for the viewer's
clarification.
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2006,
63,
1123-1126)
copyright 2006.
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