1v7m: Difference between revisions

Revision as of 02:46, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v7m.png

Template:STRUCTURE 1v7m

Human Thrombopoietin Functional Domain Complexed To Neutralizing Antibody TN1 FabHuman Thrombopoietin Functional Domain Complexed To Neutralizing Antibody TN1 Fab

Template:ABSTRACT PUBMED 14769915

About this StructureAbout this Structure

1V7M is a Single protein structure of sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

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:11976502

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OCA

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 {{STRUCTURE_1v7m|  PDB=1v7m  |  SCENE=  }}
-'''Human Thrombopoietin Functional Domain Complexed To Neutralizing Antibody TN1 Fab'''
+===Human Thrombopoietin Functional Domain Complexed To Neutralizing Antibody TN1 Fab===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14769915}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_14769915}}
 ==About this Structure==
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 ==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: Mus musculus]]
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 [[Category: Fab fragment]]
 [[Category: Thrombopoietin]]
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