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PDBsum entry 3b9c
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Unknown function
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PDB id
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3b9c
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the c-Terminal conserved domain of human grp, A galectin-Related protein, Reveals a function mode different from those of galectins.
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Authors
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D.Zhou,
H.Ge,
J.Sun,
Y.Gao,
M.Teng,
L.Niu.
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Ref.
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Proteins, 2008,
71,
1582-1588.
[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. Overall three-dimensional structure of hGRP-C. (a)
Ribbon representation of the dimer organization of hGRP-C (chain
C and chain D). Standard numbering of the secondary elements is
indicated on one polypeptide (S1-S5/F1-F5,  1).
(b) Tetramer arrangement of hGRP-C. The four monomers A, B, C,
and D are colored green, yellow, cyan, and hotpink,
respectively. The two homodimers (A,B and C,D) are approximately
perpendicular. (c) Tetramer structure of hGRP-C viewed in other
angle.
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Figure 3.
Figure 3. (a) Superposition of the architectures of
carbohydrate-recognition sites of human GRP-C and human
galectin-7. hGRP-C and hGal-7 are colored orange and blue,
respectively. hGRP-C residues E50, K52, V54, N63, R70, E73, and
S75 involved in sugar-binding and equivalent residues of hGal-7
are shown as stick models and their carbon atoms are colored
green and blue, respectively. Galactose carbon atoms are colored
gray. (b) Comparison of carbohydrate-binding pockets of hGal-7
and hGRP-C. In the left diagram, the groove labeled by a black
arrow is sugar-binding pocket of hGal-7. In the surface diagram
of hGRP-C, the region equivalent to hGal-7 binding pocket is
labeled by a black dashed pane.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
71,
1582-1588)
copyright 2008.
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