4fmf
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fmf]] 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=4FMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FMF FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fmf]] 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=4FMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FMF FirstGlance]. <br> | ||
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3.2Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4fmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmf OCA], [https://pdbe.org/4fmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fmf RCSB], [https://www.ebi.ac.uk/pdbsum/4fmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fmf 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=4fmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmf OCA], [https://pdbe.org/4fmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fmf RCSB], [https://www.ebi.ac.uk/pdbsum/4fmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fmf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
- | [https://www.uniprot.org/uniprot/NECT1_HUMAN NECT1_HUMAN] | + | [https://www.uniprot.org/uniprot/NECT1_HUMAN NECT1_HUMAN] Cleft lip/palate;Isolated cleft lip;Cleft lip and alveolus;Cleft lip/palate-ectodermal dysplasia syndrome. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. |
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NECT1_HUMAN NECT1_HUMAN] Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4. Has some neurite outgrowth-promoting activity.<ref>PMID:21980294</ref> (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV.<ref>PMID:7721102</ref> <ref>PMID:9657005</ref> | [https://www.uniprot.org/uniprot/NECT1_HUMAN NECT1_HUMAN] Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between NECTIN1 and NECTIN3 and between NECTIN1 and NECTIN4. Has some neurite outgrowth-promoting activity.<ref>PMID:21980294</ref> (Microbial infection) Acts as a receptor for herpes simplex virus 1/HHV-1, herpes simplex virus 2/HHV-2, and pseudorabies virus/PRV.<ref>PMID:7721102</ref> <ref>PMID:9657005</ref> |
Current revision
Crystal structure of human nectin-1 full ectodomain (D1-D3)
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