1h4u

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<StructureSection load='1h4u' size='340' side='right'caption='[[1h4u]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1h4u' size='340' side='right'caption='[[1h4u]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1h4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1h4u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4U FirstGlance]. <br>
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</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=1h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4u OCA], [https://pdbe.org/1h4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4u RCSB], [https://www.ebi.ac.uk/pdbsum/1h4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4u ProSAT]</span></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]] 2.2&#8491;</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=1h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4u OCA], [https://pdbe.org/1h4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4u RCSB], [https://www.ebi.ac.uk/pdbsum/1h4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NID1_MOUSE NID1_MOUSE]] Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions.
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[https://www.uniprot.org/uniprot/NID1_MOUSE NID1_MOUSE] Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions.
== 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=1h4u 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=1h4u 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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Nidogen, an invariant component of basement membranes, is a multifunctional protein that interacts with most other major basement membrane proteins. Here, we report the crystal structure of the mouse nidogen-1 G2 fragment, which contains binding sites for collagen IV and perlecan. The structure is composed of an EGF-like domain and an 11-stranded beta-barrel with a central helix. The beta-barrel domain has unexpected similarity to green fluorescent protein. A large surface patch on the beta-barrel is strikingly conserved in all metazoan nidogens. Site-directed mutagenesis demonstrates that the conserved residues are involved in perlecan binding.
 
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Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.,Hopf M, Gohring W, Ries A, Timpl R, Hohenester E Nat Struct Biol. 2001 Jul;8(7):634-40. PMID:11427896<ref>PMID:11427896</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 1h4u" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Gohring, W]]
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[[Category: Gohring W]]
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[[Category: Hohenester, E]]
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[[Category: Hohenester E]]
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[[Category: Hopf, M]]
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[[Category: Hopf M]]
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[[Category: Ries, A]]
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[[Category: Ries A]]
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[[Category: Timpl, R]]
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[[Category: Timpl R]]
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[[Category: Extracellular matrix protein]]
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Revision as of 11:28, 27 March 2024

Domain G2 of mouse nidogen-1

PDB ID 1h4u

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