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<StructureSection load='3hsh' size='340' side='right'caption='[[3hsh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3hsh' size='340' side='right'caption='[[3hsh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hsh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HSH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hsh]] is a 6 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=3HSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HSH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hon|3hon]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COL18A1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hsh OCA], [https://pdbe.org/3hsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hsh RCSB], [https://www.ebi.ac.uk/pdbsum/3hsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hsh ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hsh OCA], [https://pdbe.org/3hsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hsh RCSB], [https://www.ebi.ac.uk/pdbsum/3hsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hsh ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[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>
[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 ==
[[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.  
[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=3hsh 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=3hsh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Collagens contain a unique triple-helical structure with a repeating sequence -G-X-Y-, where proline and hydroxyproline are major constituents in X and Y positions, respectively. Folding of the collagen triple helix requires trimerization domains. Once trimerized, collagen chains are correctly aligned and the folding of the triple helix proceeds in a zipper-like fashion. Here we report the isolation, characterization, and crystal structure of the trimerization domain of human type XVIII collagen, a member of the multiplexin family. This domain differs from all other known trimerization domains in other collagens and exhibits a high trimerization potential at picomolar concentrations. Strong chain association and high specificity of binding are needed for multiplexins, which are present at very low levels.
Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold.,Boudko SP, Sasaki T, Engel J, Lerch TF, Nix J, Chapman MS, Bachinger HP J Mol Biol. 2009 Sep 25;392(3):787-802. Epub 2009 Jul 23. PMID:19631658<ref>PMID:19631658</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3hsh" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bachinger, H P]]
[[Category: Bachinger HP]]
[[Category: Boudko, S P]]
[[Category: Boudko SP]]
[[Category: Alternative promoter usage]]
[[Category: Association]]
[[Category: Basement membrane]]
[[Category: Cell adhesion]]
[[Category: Chain selection]]
[[Category: Collagen]]
[[Category: Collagen xviii]]
[[Category: Disulfide bond]]
[[Category: Endostatin]]
[[Category: Extracellular matrix]]
[[Category: Folding]]
[[Category: Glycoprotein]]
[[Category: Hydroxylation]]
[[Category: Metal-binding]]
[[Category: Protein binding]]
[[Category: Secreted]]
[[Category: Trimerization domain]]
[[Category: Triple helix]]

Latest revision as of 10:01, 21 February 2024

Crystal structure of human collagen XVIII trimerization domain (Tetragonal crystal form)

3hsh, resolution 1.80Å

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