1bwx

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(New page: 200px<br /> <applet load="1bwx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bwx" /> '''THE SOLUTION STRUCTURE OF HUMAN PARATHYROID...)
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[[Image:1bwx.gif|left|200px]]<br />
 
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'''THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39, NMR, 10 STRUCTURES'''<br />
 
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==Overview==
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==THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39, NMR, 10 STRUCTURES==
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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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<StructureSection load='1bwx' size='340' side='right'caption='[[1bwx]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bwx]] 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=1BWX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWX FirstGlance]. <br>
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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=1bwx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwx OCA], [https://pdbe.org/1bwx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwx RCSB], [https://www.ebi.ac.uk/pdbsum/1bwx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwx ProSAT]</span></td></tr>
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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/bw/1bwx_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=1bwx 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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==Disease==
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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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Known diseases associated with this structure: Hypoparathyroidism, autosomal dominant OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=168450 168450]], Hypoparathyroidism, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=168450 168450]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1BWX 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BWX OCA].
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</div>
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<div class="pdbe-citations 1bwx" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10623601 10623601]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Adermann, K.]]
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[[Category: Adermann K]]
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[[Category: Bayer, P.]]
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[[Category: Bayer P]]
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[[Category: Forssmann, W.G.]]
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[[Category: Forssmann W-G]]
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[[Category: Marx, U.C.]]
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[[Category: Marx UC]]
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[[Category: Roesch, P.]]
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[[Category: Roesch P]]
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[[Category: human parathyroid hormone]]
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[[Category: peptide hormone]]
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[[Category: solution structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:15:06 2007''
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THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE FRAGMENT 1-39, NMR, 10 STRUCTURES

PDB ID 1bwx

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