3rez

From Proteopedia

(Difference between revisions)

Revision as of 06:00, 15 June 2022

glycoprotein GPIb variant

Structural highlights

3rez is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	3rfe
Gene:	GP1BB, GP9 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[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.

Function

[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.

Publication Abstract from PubMed

Platelet GPIb-IX receptor complex has 3 subunits GPIbalpha, GPIbbeta, and GPIX, which assemble with a ratio of 1:2:1. Dysfunction in surface expression of the complex leads to Bernard-Soulier syndrome. We have crystallized the GPIbbeta ectodomain (GPIbbeta(E)) and determined the structure to show a single leucine-rich repeat with N- and C-terminal disulphide-bonded capping regions. The structure of a chimera of GPIbbeta(E) and 3 loops (a,b,c) taken from the GPIX ectodomain sequence was also determined. The chimera (GPIbbeta(Eabc)), but not GPIbbeta(E), forms a tetramer in the crystal, showing a quaternary interface between GPIbbeta and GPIX. Central to this interface is residue Tyr106 from GPIbbeta, which inserts into a pocket generated by 2 loops (b,c) from GPIX. Mutagenesis studies confirmed this interface as a valid representation of interactions between GPIbbeta and GPIX in the full-length complex. Eight GPIbbeta missense mutations identified from patients with Bernard-Soulier syndrome were examined for changes to GPIb-IX complex surface expression. Two mutations, A108P and P74R, were found to maintain normal secretion/folding of GPIbbeta(E) but were unable to support GPIX surface expression. The close structural proximity of these mutations to Tyr106 and the GPIbbeta(E) interface with GPIX indicates they disrupt the quaternary organization of the GPIb-IX complex.

Quaternary organization of GPIb-IX complex and insights into Bernard-Soulier syndrome revealed by the structures of GPIbbeta and a GPIbbeta/GPIX chimera.,McEwan PA, Yang W, Carr KH, Mo X, Zheng X, Li R, Emsley J Blood. 2011 Nov 10;118(19):5292-301. Epub 2011 Sep 8. PMID:21908432^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ McEwan PA, Yang W, Carr KH, Mo X, Zheng X, Li R, Emsley J. Quaternary organization of GPIb-IX complex and insights into Bernard-Soulier syndrome revealed by the structures of GPIbbeta and a GPIbbeta/GPIX chimera. Blood. 2011 Nov 10;118(19):5292-301. Epub 2011 Sep 8. PMID:21908432 doi:10.1182/blood-2011-05-356253

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3rez"

@@ Line 1: / Line 1: @@
 ==glycoprotein GPIb variant==
-<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 ==
-<table><tr><td colspan='2'>[[3rez]] is a 4 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=3REZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3REZ FirstGlance]. <br>
+<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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rfe|3rfe]]</td></tr>
+<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>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GP1BB, GP9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rez OCA], [http://pdbe.org/3rez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rez RCSB], [http://www.ebi.ac.uk/pdbsum/3rez PDBsum], [http://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>
 == Disease ==
-[[http://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/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.
 == Function ==
-[[http://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/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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 27: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Carr, K H]]
 [[Category: Emsley, J]]

3rez

From Proteopedia

Revision as of 06:00, 15 June 2022

glycoprotein GPIb variant

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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