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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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Contents |
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* Residue conservation analysis
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PDB id:
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Unknown function
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Title:
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Crystal structure of human grp crd
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Structure:
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Hspc159. Chain: a, d, c, b. Fragment: unp residues 38-172. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.90Å
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R-factor:
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0.224
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R-free:
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0.266
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Authors:
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D.Zhou,H.H.Ge,L.W.Niu,M.K.Teng
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Key ref:
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D.Zhou
et al.
(2008).
Crystal structure of the C-terminal conserved domain of human GRP, a galectin-related protein, reveals a function mode different from those of galectins.
Proteins,
71,
1582-1588.
PubMed id:
DOI:
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Date:
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05-Nov-07
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Release date:
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18-Mar-08
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PROCHECK
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Headers
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References
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Q3ZCW2
(LEGL_HUMAN) -
Galectin-related protein from Homo sapiens
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Seq:
Struc:
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172 a.a.
134 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Proteins
71:1582-1588
(2008)
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PubMed id:
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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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D.Zhou,
H.Ge,
J.Sun,
Y.Gao,
M.Teng,
L.Niu.
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ABSTRACT
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Selected figure(s)
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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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Figures were
selected
by an automated process.
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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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E.d.e. .P.Mendonça-Franqueiro,
R.d.e. .M.Alves-Paiva,
M.A.Sartim,
D.R.Callejon,
H.H.Paiva,
G.A.Antonucci,
J.C.Rosa,
A.C.Cintra,
J.J.Franco,
E.C.Arantes,
M.Dias-Baruffi,
and
S.V.Sampaio
(2011).
Isolation, functional, and partial biochemical characterization of galatrox, an acidic lectin from Bothrops atrox snake venom.
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Acta Biochim Biophys Sin (Shanghai),
43,
181-192.
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G.R.Vasta
(2009).
Roles of galectins in infection.
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Nat Rev Microbiol,
7,
424-438.
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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.
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Links
