1hth
From Proteopedia
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- | [[Image:1hth.gif|left|200px]] | + | [[Image:1hth.gif|left|200px]] |
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- | '''THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES''' | + | {{Structure |
+ | |PDB= 1hth |SIZE=350|CAPTION= <scene name='initialview01'>1hth</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1HTH is a [ | + | 1HTH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTH OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10050767 10050767] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ornithine]] | [[Category: ornithine]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:22 2008'' |
Revision as of 09:41, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Hypoparathyroidism, autosomal dominant OMIM:[168450], Hypoparathyroidism, autosomal recessive OMIM:[168450]
About this Structure
1HTH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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