1zwa

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{{Seed}}
 
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[[Image:1zwa.png|left|200px]]
 
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==STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1zwa", creates the "Structure Box" on the page.
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<StructureSection load='1zwa' size='340' side='right'caption='[[1zwa]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1zwa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZWA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1zwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zwa OCA], [https://pdbe.org/1zwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zwa RCSB], [https://www.ebi.ac.uk/pdbsum/1zwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zwa ProSAT]</span></td></tr>
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{{STRUCTURE_1zwa| PDB=1zwa | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PTHY_HUMAN PTHY_HUMAN] Defects in PTH are a cause of familial isolated hypoparathyroidism (FIH) [MIM:[https://omim.org/entry/146200 146200]; also called autosomal dominant hypoparathyroidism or autosomal dominant hypocalcemia. FIH is characterized by hypocalcemia and hyperphosphatemia due to inadequate secretion of parathyroid hormone. Symptoms are seizures, tetany and cramps. FIH exist both as autosomal dominant and recessive forms of hypoparathyroidism.<ref>PMID:2212001</ref> <ref>PMID:10523031</ref> <ref>PMID:18056632</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/PTHY_HUMAN PTHY_HUMAN] PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells.<ref>PMID:21076856</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zw/1zwa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1zwa ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Parathyroid hormone (PTH) is involved in regulation of the calcium level in blood and has an influence on bone metabolism, thus playing a role in osteoporosis therapy. In this study, the structures of the human PTH fragments (1-34) and (1-39) as well as bovine PTH(1-37) in aqueous buffer solution under near physiological conditions were determined using two-dimensional nuclear magnetic resonance spectroscopy. The overall structure of the first 34 amino acids of these three peptides is virtually identical, exhibiting a short NH(2)-terminal and a longer COOH-terminal helix as well as a defined loop region from His14 to Ser17, stabilized by hydrophobic interactions. bPTH(1-37), which has a higher biological activity, shows a better-defined NH(2)-terminal part. In contrast to NH(2)-terminal truncations, which cause destabilization of helical structure, neither COOH-terminal truncation nor elongation significantly influences the secondary structure. Furthermore, we investigated the structure of hPTH(1-34) in 20% trifluoroethanol solution. In addition to its helix-stabilizing effect, trifluorethanol causes the loss of tertiary hydrophobic interactions.
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===STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES===
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Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37).,Marx UC, Adermann K, Bayer P, Forssmann WG, Rosch P Biochem Biophys Res Commun. 2000 Jan 7;267(1):213-20. PMID:10623601<ref>PMID:10623601</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_10623601}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1zwa" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10623601 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10623601}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1ZWA is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWA OCA].
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==Reference==
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<ref group="xtra">PMID:10623601</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Marx, U C.]]
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[[Category: Large Structures]]
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[[Category: Roesch, P.]]
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[[Category: Marx UC]]
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[[Category: Disease mutation]]
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[[Category: Roesch P]]
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[[Category: Hormone]]
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[[Category: Signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:36:53 2009''
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Current revision

STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES

PDB ID 1zwa

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