1v7m: Difference between revisions

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-{{Seed}}
-[[Image:1v7m.png|left|200px]]
-<!--
+==Human Thrombopoietin Functional Domain Complexed To Neutralizing Antibody TN1 Fab==
-The line below this paragraph, containing "STRUCTURE_1v7m", creates the "Structure Box" on the page.
+<StructureSection load='1v7m' size='340' side='right'caption='[[1v7m]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1v7m]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V7M FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</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=1v7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7m OCA], [https://pdbe.org/1v7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v7m RCSB], [https://www.ebi.ac.uk/pdbsum/1v7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v7m ProSAT]</span></td></tr>
-{{STRUCTURE_1v7m|  PDB=1v7m  |  SCENE=  }}
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/TPO_HUMAN TPO_HUMAN] Defects in THPO are the cause of thrombocythemia type 1 (THCYT1) [MIM:[https://omim.org/entry/187950 187950]. A myeloproliferative disorder characterized by elevated platelet levels due to sustained proliferation of megakaryocytes, and frequently lead to thrombotic and haemorrhagic complications.<ref>PMID:9425899</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/TPO_HUMAN TPO_HUMAN] Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets.
+== 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/v7/1v7m_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1v7m ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The cytokine thrombopoietin (TPO), the ligand for the hematopoietic receptor c-Mpl, acts as a primary regulator of megakaryocytopoiesis and platelet production. We have determined the crystal structure of the receptor-binding domain of human TPO (hTPO(163)) to a 2.5-A resolution by complexation with a neutralizing Fab fragment. The backbone structure of hTPO(163) has an antiparallel four-helix bundle fold. The neutralizing Fab mainly recognizes the C-D crossover loop containing the species invariant residue Q111. Titration calorimetric experiments show that hTPO(163) interacts with soluble c-Mpl containing the extracellular cytokine receptor homology domains with 1:2 stoichiometry with the binding constants of 3.3 x 10(9) M(-1) and 1.1 x 10(6) M(-1). The presence of the neutralizing Fab did not inhibit binding of hTPO(163) to soluble c-Mpl fragments, but the lower-affinity binding disappeared. Together with prior genetic data, these define the structure-function relationships in TPO and the activation scheme of c-Mpl.
-===Human Thrombopoietin Functional Domain Complexed To Neutralizing Antibody TN1 Fab===
+Structure of the receptor-binding domain of human thrombopoietin determined by complexation with a neutralizing antibody fragment.,Feese MD, Tamada T, Kato Y, Maeda Y, Hirose M, Matsukura Y, Shigematsu H, Muto T, Matsumoto A, Watarai H, Ogami K, Tahara T, Kato T, Miyazaki H, Kuroki R Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1816-21. Epub 2004 Feb 9. PMID:14769915<ref>PMID:14769915</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1v7m" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_14769915}}, adds the Publication Abstract to the page
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 14769915 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_14769915}}
+__TOC__
+</StructureSection>
-==About this Structure==
-V7M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7M OCA].
-==Reference==
-Structure of the receptor-binding domain of human thrombopoietin determined by complexation with a neutralizing antibody fragment., Feese MD, Tamada T, Kato Y, Maeda Y, Hirose M, Matsukura Y, Shigematsu H, Muto T, Matsumoto A, Watarai H, Ogami K, Tahara T, Kato T, Miyazaki H, Kuroki R, Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1816-21. Epub 2004 Feb 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14769915 14769915]
-Crystallization of the functional domain of human thrombopoietin using an antigen-binding fragment derived from neutralizing monoclonal antibody., Kuroki R, Hirose M, Kato Y, Feese MD, Tamada T, Shigematsu H, Watarai H, Maeda Y, Tahara T, Kato T, Miyazaki H, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):856-8. Epub 2002, Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11976502 11976502]
 [[Category: Homo sapiens]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Feese MD]]
-[[Category: Feese, M D.]]
+[[Category: Hirose M]]
-[[Category: Hirose, M.]]
+[[Category: Kato T]]
-[[Category: Kato, T.]]
+[[Category: Kato Y]]
-[[Category: Kato, Y.]]
+[[Category: Kuroki R]]
-[[Category: Kuroki, R.]]
+[[Category: Maeda Y]]
-[[Category: Maeda, Y.]]
+[[Category: Matsukura Y]]
-[[Category: Matsukura, Y.]]
+[[Category: Miyazaki H]]
-[[Category: Miyazaki, H.]]
+[[Category: Shigematsu H]]
-[[Category: Shigematsu, H.]]
+[[Category: Tamada T]]
-[[Category: Tamada, T.]]
-[[Category: Fab fragment]]
-[[Category: Thrombopoietin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:46:36 2008''