6xe6

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Current revision (05:57, 21 November 2024) (edit) (undo)
 
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<StructureSection load='6xe6' size='340' side='right'caption='[[6xe6]], [[Resolution|resolution]] 4.54&Aring;' scene=''>
<StructureSection load='6xe6' size='340' side='right'caption='[[6xe6]], [[Resolution|resolution]] 4.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6xe6]] is a 1 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=6XE6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XE6 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XE6 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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</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">Electron Microscopy, [[Resolution|Resolution]] 4.54&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DISP1, DISPA ([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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</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=6xe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xe6 OCA], [http://pdbe.org/6xe6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xe6 RCSB], [http://www.ebi.ac.uk/pdbsum/6xe6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xe6 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=6xe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xe6 OCA], [https://pdbe.org/6xe6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xe6 RCSB], [https://www.ebi.ac.uk/pdbsum/6xe6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xe6 ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/DISP1_HUMAN DISP1_HUMAN]] Septopreoptic holoprosencephaly;Alobar holoprosencephaly;Semilobar holoprosencephaly;Lobar holoprosencephaly;Midline interhemispheric variant of holoprosencephaly;Microform holoprosencephaly.
 
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== Function ==
 
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[[http://www.uniprot.org/uniprot/DISP1_HUMAN DISP1_HUMAN]] Functions in hedgehog (Hh) signaling. Regulates the release and extracellular accumulation of cholesterol-modified hedgehog proteins and is hence required for effective production of the Hh signal (By similarity). Synergizes with SCUBE2 to cause an increase in SHH secretion (PubMed:22902404).[UniProtKB:Q3TDN0]<ref>PMID:22902404</ref>
 
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Hedgehog (HH) signaling is essential for metazoan development. The HH ligand is secreted into the extracellular space by a cell surface protein named Dispatched-1 (DISP1). Here, we report the cryo-EM structure of human DISP1 protein. DISP1 contains 12 transmembrane helices (TMs) and two extracellular domains (ECDs). Its ECDs reveal an open state, in contrast to its structural homologues PTCH1 and NPC1, whose extracellular/luminal domains adopt a closed state. The low-resolution structure of the DISP1 complex with dual lipid-modified HH ligand reveals how the ECDs of DISP1 engage with HH ligand. Moreover, several cholesterol-like molecules are found in the TMs, implying a transport-like function of DISP1.
 
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Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.,Chen H, Liu Y, Li X Life Sci Alliance. 2020 Jul 9;3(8). pii: 3/8/e202000776. doi:, 10.26508/lsa.202000776. Print 2020 Aug. PMID:32646883<ref>PMID:32646883</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 6xe6" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, H]]
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[[Category: Chen H]]
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[[Category: Li, X]]
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[[Category: Li X]]
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[[Category: Liu, Y]]
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[[Category: Liu Y]]
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[[Category: Hedgehog]]
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[[Category: Membrane protein]]
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[[Category: Secretion]]
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[[Category: Sterol binding]]
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[[Category: Sterol-sensing domain]]
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Current revision

Structure of Human Dispatched-1 (DISP1)

PDB ID 6xe6

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