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PDBsum entry 1bnl
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Extracellular matrix
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PDB id
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1bnl
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Zinc-Dependent dimers observed in crystals of human endostatin.
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Authors
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Y.H.Ding,
K.Javaherian,
K.M.Lo,
R.Chopra,
T.Boehm,
J.Lanciotti,
B.A.Harris,
Y.Li,
R.Shapiro,
E.Hohenester,
R.Timpl,
J.Folkman,
D.C.Wiley.
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Ref.
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Proc Natl Acad Sci U S A, 1998,
95,
10443-10448.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of human endostatin reveals a zinc-binding site. Atomic
absorption spectroscopy indicates that zinc is a constituent of both human and
murine endostatin in solution. The human endostatin zinc site is formed by three
histidines at the N terminus, residues 1, 3, and, 11, and an aspartic acid at
residue 76. The N-terminal loop ordered around the zinc makes a dimeric contact
in human endostatin crystals. The location of the zinc site at the amino
terminus, immediately adjacent to the precursor cleavage site, suggests the
possibility that the zinc may be involved in activation of the antiangiogenic
activity following cleavage from the inactive collagen XVIII precursor or in the
cleavage process itself.
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Figure 1.
Fig. 1. The structure of human endostatin.  -strands
(cyan) are labeled in sequential order A-P,  helices
are violet, and connecting loops are pink. Residues 1-6 are
blue; zinc is a black circle. Human and murine endostatin are
very similar (rms deviation = 0.46 Å for 196 C pairs; cf.
Fig. 3B in ref. 3).
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Figure 4.
Fig. 4. A positively charged surface formed by arginines
on the human endostatin dimer. Stereo diagram, surface
glutamines (yellow), asparagines (cyan), lysines (green), and
arginines (blue) are shown.
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