1hth
From Proteopedia
(New page: 200px<br /> <applet load="1hth" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hth" /> '''THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARA...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1hth.gif|left|200px]]<br /> | + | [[Image:1hth.gif|left|200px]]<br /><applet load="1hth" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1hth" size=" | + | |
caption="1hth" /> | caption="1hth" /> | ||
'''THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES'''<br /> | '''THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
- | Parathyroid hormone-related protein plays a major role in the pathogenesis | + | 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== | ==Disease== | ||
Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
- | 1HTH 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:// | + | 1HTH 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTH OCA]. |
==Reference== | ==Reference== | ||
Line 28: | Line 27: | ||
[[Category: ornithine]] | [[Category: ornithine]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:39 2008'' |
Revision as of 11:04, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 13:04:39 2008