1dy0: Difference between revisions

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[[Image:1dy0.gif|left|200px]]
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[[Image:1dy0.png|left|200px]]


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{{STRUCTURE_1dy0|  PDB=1dy0  |  SCENE=  }}  
{{STRUCTURE_1dy0|  PDB=1dy0  |  SCENE=  }}  


'''MURINE ENDOSTATIN, CRYSTAL FORM II'''
===MURINE ENDOSTATIN, CRYSTAL FORM II===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10704302}}


==About this Structure==
==About this Structure==
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[[Category: Timpl, R.]]
[[Category: Timpl, R.]]
[[Category: Angiogenesis inhibitor]]
[[Category: Angiogenesis inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:47:20 2008''

Revision as of 23:47, 30 June 2008

File:1dy0.png

Template:STRUCTURE 1dy0

MURINE ENDOSTATIN, CRYSTAL FORM IIMURINE ENDOSTATIN, CRYSTAL FORM II

Template:ABSTRACT PUBMED 10704302

About this StructureAbout this Structure

1DY0 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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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