1bnl

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<StructureSection load='1bnl' size='340' side='right'caption='[[1bnl]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='1bnl' size='340' side='right'caption='[[1bnl]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1bnl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BNL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1bnl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BNL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COLLAGEN XVIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bnl OCA], [http://pdbe.org/1bnl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bnl RCSB], [http://www.ebi.ac.uk/pdbsum/1bnl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bnl ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bnl OCA], [https://pdbe.org/1bnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bnl RCSB], [https://www.ebi.ac.uk/pdbsum/1bnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bnl ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/COIA1_HUMAN COIA1_HUMAN]] Defects in COL18A1 are a cause of Knobloch syndrome type 1 (KNO1) [MIM:[http://omim.org/entry/267750 267750]]. An autosomal recessive disorder defined by the occurrence of high myopia, vitreoretinal degeneration with retinal detachment, macular abnormalities and occipital encephalocele.<ref>PMID:10942434</ref>
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[https://www.uniprot.org/uniprot/COIA1_HUMAN COIA1_HUMAN] Defects in COL18A1 are a cause of Knobloch syndrome type 1 (KNO1) [MIM:[https://omim.org/entry/267750 267750]. An autosomal recessive disorder defined by the occurrence of high myopia, vitreoretinal degeneration with retinal detachment, macular abnormalities and occipital encephalocele.<ref>PMID:10942434</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/COIA1_HUMAN COIA1_HUMAN]] COLA18A probably plays a major role in determining the retinal structure as well as in the closure of the neural tube. Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling.
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[https://www.uniprot.org/uniprot/COIA1_HUMAN COIA1_HUMAN] COLA18A probably plays a major role in determining the retinal structure as well as in the closure of the neural tube. Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bnl ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bnl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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Zinc-dependent dimers observed in crystals of human endostatin.,Ding YH, Javaherian K, Lo KM, Chopra R, Boehm T, Lanciotti J, Harris BA, Li Y, Shapiro R, Hohenester E, Timpl R, Folkman J, Wiley DC Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10443-8. PMID:9724722<ref>PMID:9724722</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1bnl" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Boehm, T]]
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[[Category: Boehm T]]
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[[Category: Chopra, R]]
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[[Category: Chopra R]]
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[[Category: Ding, Y H]]
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[[Category: Ding Y-H]]
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[[Category: Folkman, J]]
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[[Category: Folkman J]]
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[[Category: Harris, B A]]
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[[Category: Harris BA]]
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[[Category: Hohenester, E]]
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[[Category: Hohenester E]]
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[[Category: Javaherian, K]]
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[[Category: Javaherian K]]
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[[Category: Lanciotti, J]]
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[[Category: Lanciotti J]]
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[[Category: Li, Y]]
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[[Category: Li Y]]
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[[Category: Lo, K M]]
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[[Category: Lo K-M]]
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[[Category: Shapiro, R]]
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[[Category: Shapiro R]]
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[[Category: Timpl, R]]
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[[Category: Timpl R]]
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[[Category: Wiley, D C]]
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[[Category: Wiley DC]]
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[[Category: Angiogenic]]
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[[Category: Angiogenisis]]
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[[Category: Antiangiogenic]]
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[[Category: Cancer]]
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[[Category: Collagen]]
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[[Category: Collagen xviii]]
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[[Category: Endostatin]]
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[[Category: Extracellular matrix]]
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[[Category: Zinc]]
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Revision as of 15:34, 13 March 2024

ZINC DEPENDENT DIMERS OBSERVED IN CRYSTALS OF HUMAN ENDOSTATIN

PDB ID 1bnl

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