1et1: Difference between revisions
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|PDB= 1et1 |SIZE=350|CAPTION= <scene name='initialview01'>1et1</scene>, resolution 0.90Å | |PDB= 1et1 |SIZE=350|CAPTION= <scene name='initialview01'>1et1</scene>, resolution 0.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1et1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1et1 OCA], [http://www.ebi.ac.uk/pdbsum/1et1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1et1 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Tashjian, A H.]] | [[Category: Tashjian, A H.]] | ||
[[Category: Zhang, F.]] | [[Category: Zhang, F.]] | ||
[[Category: helical dimer]] | [[Category: helical dimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:09:06 2008'' | ||
