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1et1

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(New page: 200px<br /> <applet load="1et1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1et1, resolution 0.90&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1et1.gif|left|200px]]<br /><applet load="1et1" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1et1" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1et1, resolution 0.90&Aring;" />
caption="1et1, resolution 0.90&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN PARATHYROID HORMONE 1-34 AT 0.9 A RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF HUMAN PARATHYROID HORMONE 1-34 AT 0.9 A RESOLUTION'''<br />
==Overview==
==Overview==
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The N-terminal fragment 1-34 of parathyroid hormone (PTH), administered, intermittently, results in increased bone formation in patients with, osteoporosis. PTH and a related molecule, parathyroid hormone-related, peptide (PTHrP), act on cells via a common PTH/PTHrP receptor. To define, more precisely the ligand-receptor interactions, we have crystallized, human PTH (hPTH)-(1-34) and determined the structure to 0.9-A resolution., hPTH-(1-34) crystallizes as a slightly bent, long helical dimer. Analysis, reveals that the extended helical conformation of hPTH-(1-34) is the, likely bioactive conformation. We have developed molecular models for the, interaction of hPTH-(1-34) and hPTHrP-(1-34) with the PTH/PTHrP receptor., A receptor binding pocket for the N terminus of hPTH-(1-34) and a, hydrophobic interface with the receptor for the C terminus of hPTH-(1-34), are proposed.
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The N-terminal fragment 1-34 of parathyroid hormone (PTH), administered intermittently, results in increased bone formation in patients with osteoporosis. PTH and a related molecule, parathyroid hormone-related peptide (PTHrP), act on cells via a common PTH/PTHrP receptor. To define more precisely the ligand-receptor interactions, we have crystallized human PTH (hPTH)-(1-34) and determined the structure to 0.9-A resolution. hPTH-(1-34) crystallizes as a slightly bent, long helical dimer. Analysis reveals that the extended helical conformation of hPTH-(1-34) is the likely bioactive conformation. We have developed molecular models for the interaction of hPTH-(1-34) and hPTHrP-(1-34) with the PTH/PTHrP receptor. A receptor binding pocket for the N terminus of hPTH-(1-34) and a hydrophobic interface with the receptor for the C terminus of hPTH-(1-34) are proposed.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1ET1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ET1 OCA].
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1ET1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ET1 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Briggs, S.L.]]
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[[Category: Briggs, S L.]]
[[Category: Chandrasekhar, S.]]
[[Category: Chandrasekhar, S.]]
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[[Category: Chirgadze, N.Y.]]
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[[Category: Chirgadze, N Y.]]
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[[Category: Clawson, D.K.]]
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[[Category: Clawson, D K.]]
[[Category: Jin, L.]]
[[Category: Jin, L.]]
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[[Category: Schevitz, R.W.]]
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[[Category: Schevitz, R W.]]
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[[Category: Smiley, D.L.]]
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[[Category: Smiley, D L.]]
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[[Category: Tashjian, A.H.]]
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[[Category: Tashjian, A H.]]
[[Category: Zhang, F.]]
[[Category: Zhang, F.]]
[[Category: NA]]
[[Category: NA]]
[[Category: helical dimer]]
[[Category: helical dimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:46:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:13 2008''

Revision as of 10:31, 21 February 2008


1et1, resolution 0.90Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF HUMAN PARATHYROID HORMONE 1-34 AT 0.9 A RESOLUTION

Contents

Overview

The N-terminal fragment 1-34 of parathyroid hormone (PTH), administered intermittently, results in increased bone formation in patients with osteoporosis. PTH and a related molecule, parathyroid hormone-related peptide (PTHrP), act on cells via a common PTH/PTHrP receptor. To define more precisely the ligand-receptor interactions, we have crystallized human PTH (hPTH)-(1-34) and determined the structure to 0.9-A resolution. hPTH-(1-34) crystallizes as a slightly bent, long helical dimer. Analysis reveals that the extended helical conformation of hPTH-(1-34) is the likely bioactive conformation. We have developed molecular models for the interaction of hPTH-(1-34) and hPTHrP-(1-34) with the PTH/PTHrP receptor. A receptor binding pocket for the N terminus of hPTH-(1-34) and a hydrophobic interface with the receptor for the C terminus of hPTH-(1-34) are proposed.

Disease

Known diseases associated with this structure: Hypoparathyroidism, autosomal dominant OMIM:[168450], Hypoparathyroidism, autosomal recessive OMIM:[168450]

About this Structure

1ET1 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution., Jin L, Briggs SL, Chandrasekhar S, Chirgadze NY, Clawson DK, Schevitz RW, Smiley DL, Tashjian AH, Zhang F, J Biol Chem. 2000 Sep 1;275(35):27238-44. PMID:10837469

Page seeded by OCA on Thu Feb 21 12:31:13 2008

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