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==The solution structure of cyclic human parathyroid hormone fragment 1-34, NMR, 10 structures==
==The solution structure of cyclic human parathyroid hormone fragment 1-34, NMR, 10 structures==
<StructureSection load='1hth' size='340' side='right' caption='[[1hth]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1hth' size='340' side='right'caption='[[1hth]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hth]] is a 1 chain structure with 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=1HTH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HTH FirstGlance]. <br>
<table><tr><td colspan='2'>[[1hth]] 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=1HTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTH FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hth OCA], [http://pdbe.org/1hth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hth RCSB], [http://www.ebi.ac.uk/pdbsum/1hth PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hth ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</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=1hth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hth OCA], [https://pdbe.org/1hth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hth RCSB], [https://www.ebi.ac.uk/pdbsum/1hth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hth ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/PTHY_HUMAN PTHY_HUMAN]] Defects in PTH are a cause of familial isolated hypoparathyroidism (FIH) [MIM:[http://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>
[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>  
== Function ==
== Function ==
[[http://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>
[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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1hth ConSurf].
</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=1hth ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Parathyroid hormone-related protein plays a major role in the pathogenesis of humoral hypercalcemia of malignancy. Under normal physiological conditions, parathyroid hormone-related protein is produced in a wide variety of tissues and acts in an autocrine or paracrine fashion. Parathyroid hormone-related protein and parathyroid hormone bind to and activate the same G-protein-coupled receptor. Here we present the structure of the biologically active NH2-terminal domain of human parathyroid hormone-related protein(1-34) in near-physiological solution in the absence of crowding reagents as determined by two-dimensional proton magnetic resonance spectroscopy. An improved strategy for structure calculation revealed the presence of two helices, His-5-Leu-8 and Gln-16-Leu-27, connected by a flexible linker. The parathyroid hormone-related protein(1-34) structure and the structure of human parathyroid hormone(1-37) as well as human parathyroid hormone(1-34) are highly similar, except for the well defined turn, His-14-Ser-17, present in parathyroid hormone. Thus, the similarity of the binding affinities of parathyroid hormone and parathyroid hormone-related protein to their common receptor may be based on their structural similarity.
The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution.,Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P FEBS Lett. 1999 Feb 12;444(2-3):239-44. PMID:10050767<ref>PMID:10050767</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hth" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Esswein, A]]
[[Category: Large Structures]]
[[Category: Hofmann, E]]
[[Category: Esswein A]]
[[Category: Roesch, P]]
[[Category: Hofmann E]]
[[Category: Schaefer, W]]
[[Category: Roesch P]]
[[Category: Seidel, G]]
[[Category: Schaefer W]]
[[Category: Cyclic]]
[[Category: Seidel G]]
[[Category: Hormone]]
[[Category: Human parathyroid hormone]]
[[Category: Norleucine]]
[[Category: Ornithine]]
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