1ET1

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

Summary for 1ET1

• Entry DOI: 10.2210/pdb1et1/pdb
• Descriptor: PARATHYROID HORMONE, SODIUM ION (3 entities in total)
• Functional Keywords: helical dimer, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P01270
• Total number of polymer chains: 2
• Total formula weight: 8297.54

Authors

Jin, L.,Briggs, S.L.,Chandrasekhar, S.,Chirgadze, N.Y.,Clawson, D.K.,Schevitz, R.W.,Smiley, D.L.,Tashjian, A.H.,Zhang, F. (deposition date: 2000-04-12, release date: 2000-09-06, Last modification date: 2024-02-07)

Primary citation

Jin, L.,Briggs, S.L.,Chandrasekhar, S.,Chirgadze, N.Y.,Clawson, D.K.,Schevitz, R.W.,Smiley, D.L.,Tashjian, A.H.,Zhang, F.
Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution.
J.Biol.Chem., 275:27238-27244, 2000

PubMed Abstract: 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.

PubMed: 10837469

Experimental method

X-RAY DIFFRACTION (0.9 Å)