1hth: Difference between revisions

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[[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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1hth" />

'''THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES'''<br />

==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.

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==

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==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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1HTH OCA].

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==

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[[Category: ornithine]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:39 2008''

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-[[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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1hth" />
 '''THE SOLUTION STRUCTURE OF CYCLIC HUMAN PARATHYROID HORMONE FRAGMENT 1-34, NMR, 10 STRUCTURES'''<br />
 ==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.
+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==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-HTH 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=1HTH OCA].
+HTH 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==
@@ Line 28: / Line 27: @@
 [[Category: ornithine]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:22:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:39 2008''