3rez

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Current revision (06:08, 17 October 2024) (edit) (undo)
 
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<StructureSection load='3rez' size='340' side='right'caption='[[3rez]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3rez' size='340' side='right'caption='[[3rez]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rez]] is a 4 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=3REZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3REZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rez]] 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=3REZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3REZ 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=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.35&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rfe|3rfe]]</div></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=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GP1BB, GP9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3rez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rez OCA], [https://pdbe.org/3rez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rez RCSB], [https://www.ebi.ac.uk/pdbsum/3rez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rez 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=3rez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rez OCA], [https://pdbe.org/3rez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rez RCSB], [https://www.ebi.ac.uk/pdbsum/3rez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rez ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/GP1BB_HUMAN GP1BB_HUMAN]] Bernard-Soulier syndrome;22q11.2 deletion syndrome;Fetal and neonatal alloimmune thrombocytopenia. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/GP1BB_HUMAN GP1BB_HUMAN] Bernard-Soulier syndrome;22q11.2 deletion syndrome;Fetal and neonatal alloimmune thrombocytopenia. The disease is caused by mutations affecting the gene represented in this entry.[https://www.uniprot.org/uniprot/GPIX_HUMAN GPIX_HUMAN] Bernard-Soulier syndrome. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GP1BB_HUMAN GP1BB_HUMAN]] Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.
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[https://www.uniprot.org/uniprot/GP1BB_HUMAN GP1BB_HUMAN] Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.[https://www.uniprot.org/uniprot/GPIX_HUMAN GPIX_HUMAN] The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib.
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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: Carr, K H]]
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[[Category: Carr KH]]
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[[Category: Emsley, J]]
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[[Category: Emsley J]]
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[[Category: Li, R]]
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[[Category: Li R]]
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[[Category: McEwan, P A]]
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[[Category: McEwan PA]]
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[[Category: Mo, X]]
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[[Category: Mo X]]
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[[Category: Yang, W]]
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[[Category: Yang W]]
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[[Category: Zheng, X]]
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[[Category: Zheng X]]
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[[Category: Cell adhesion]]
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[[Category: Glycoprotein]]
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[[Category: Gp1bb and gpix]]
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[[Category: Platelet surface receptor]]
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Current revision

glycoprotein GPIb variant

PDB ID 3rez

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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