1p9a: Difference between revisions

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-[[Image:1p9a.jpg|left|200px]]<br /><applet load="1p9a" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1p9a, resolution 1.7&Aring;" />
-'''Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution'''<br />
-==Overview==
+==Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution==
-Thrombin bound to platelets contributes to stop bleeding and, in, pathological conditions, may cause vascular thrombosis. We have determined, the structure of platelet glycoprotein Ibalpha (GpIbalpha) bound to, thrombin at 2.3 angstrom resolution and defined two sites in GpIbalpha, that bind to exosite II and exosite I of two distinct alpha-thrombin, molecules, respectively. GpIbalpha occupancy may be sequential, as the, site binding to alpha-thrombin exosite I appears to be cryptic in the, unoccupied receptor but exposed when a first thrombin molecule is bound, through exosite II. These interactions may modulate alpha-thrombin, function by mediating GpIbalpha clustering and cleavage of, protease-activated receptors, which promote platelet activation, while, limiting fibrinogen clotting through blockade of exosite I.
+<StructureSection load='1p9a' size='340' side='right'caption='[[1p9a]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1p9a]] is a 1 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=1P9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P9A FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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=1p9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9a OCA], [https://pdbe.org/1p9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p9a RCSB], [https://www.ebi.ac.uk/pdbsum/1p9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9a ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/GP1BA_HUMAN GP1BA_HUMAN] Genetic variations in GP1BA may be a cause of susceptibility to non-arteritic anterior ischemic optic neuropathy (NAION) [MIM:[https://omim.org/entry/258660 258660]. NAION is an ocular disease due to ischemic injury to the optic nerve. It usually affects the optic disk and leads to visual loss and optic disk swelling of a pallid nature. Visual loss is usually sudden, or over a few days at most and is usually permanent, with some recovery possibly occurring within the first weeks or months. Patients with small disks having smaller or non-existent cups have an anatomical predisposition for non-arteritic anterior ischemic optic neuropathy. As an ischemic episode evolves, the swelling compromises circulation, with a spiral of ischemia resulting in further neuronal damage.<ref>PMID:14711733</ref>   Defects in GP1BA are a cause of Bernard-Soulier syndrome (BSS) [MIM:[https://omim.org/entry/231200 231200]; also known as giant platelet disease (GPD). BSS patients have unusually large platelets and have a clinical bleeding tendency.<ref>PMID:1730088</ref> <ref>PMID:7690774</ref> <ref>PMID:7819107</ref> <ref>PMID:7873390</ref> <ref>PMID:9639514</ref> <ref>PMID:10089893</ref>   Defects in GP1BA are the cause of benign mediterranean macrothrombocytopenia (BMM) [MIM:[https://omim.org/entry/153670 153670]; also known as autosomal dominant benign Bernard-Soulier syndrome. BMM is characterized by mild or no clinical symptoms, normal platelet function, and normal megakaryocyte count.<ref>PMID:11222377</ref>   Defects in GP1BA are the cause of pseudo-von Willebrand disease (VWDP) [MIM:[https://omim.org/entry/177820 177820]. A bleeding disorder is caused by an increased affinity of GP-Ib for soluble vWF resulting in impaired hemostatic function due to the removal of vWF from the circulation.<ref>PMID:14521605</ref> <ref>PMID:2052556</ref> <ref>PMID:8486780</ref> <ref>PMID:8384898</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/GP1BA_HUMAN GP1BA_HUMAN] GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p9/1p9a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1p9a ConSurf].
+<div style="clear:both"></div>
-==Disease==
+==See Also==
-Known diseases associated with this structure: Bernard-Soulier syndrome, type A OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]], Nonarteritic anterior ischemic optic neuropathy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]], von Willebrand disease, platelet-type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606672 606672]]
+*[[Platelet glycoprotein|Platelet glycoprotein]]
+== References ==
-==About this Structure==
+<references/>
-P9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9A OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha., Celikel R, McClintock RA, Roberts JR, Mendolicchio GL, Ware J, Varughese KI, Ruggeri ZM, Science. 2003 Jul 11;301(5630):218-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12855810 12855810]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Celikel, R.]]
+[[Category: Celikel R]]
-[[Category: Ruggeri, Z.M.]]
+[[Category: Ruggeri ZM]]
-[[Category: Varughese, K.I.]]
+[[Category: Varughese KI]]
-[[Category: glycocalicin]]
-[[Category: leucine rich repeats]]
-[[Category: platelet receptors]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:39:23 2008''