1dy0
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(New page: 200px<br /><applet load="1dy0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dy0, resolution 2.20Å" /> '''MURINE ENDOSTATIN, C...)
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Revision as of 11:32, 20 November 2007
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MURINE ENDOSTATIN, CRYSTAL FORM II
Overview
Endostatin is a proteolytic fragment of collagen XVIII that potently, inhibits angiogenesis and tumour growth. Human endostatin contains a zinc, ion, bound near the N terminus, which was not observed in the original, structure of mouse endostatin at pH 5. Controversial data exist on the, role of this zinc ion in the anti-tumour activity. We report two new, crystal structures of mouse endostatin at pH 8.5 with bound zinc. One, crystal form shows a metal ion coordination similar to that in human, endostatin (His132, His134, His142, Asp207), but the conformation of the, N-terminal segment is different. In the other crystal form, Asp136, replaces His132 as a zinc ligand. Site-directed mutagenesis of, zinc-binding residues demonstrates that both coordination geometries occur, in solution. The large degree of structural heterogeneity of the, zinc-binding site has implications for endostatin function. We conclude, that zinc is likely to play a structural rather than a critical functional, role in endostatin.
About this Structure
1DY0 is a Single protein structure of sequence from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Variable zinc coordination in endostatin., Hohenester E, Sasaki T, Mann K, Timpl R, J Mol Biol. 2000 Mar 17;297(1):1-6. PMID:10704302
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