1HTH

The solution structure of cyclic human parathyroid hormone fragment 1-34, NMR, 10 structures

Summary for 1HTH

• Entry DOI: 10.2210/pdb1hth/pdb
• Descriptor: CYCLIC PARATHYROID HORMONE (1 entity in total)
• Functional Keywords: human parathyroid hormone, cyclic, ornithine, norleucine, hormone
• Biological source: Homo sapiens (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 4116.70

Authors

Roesch, P.,Seidel, G.,Schaefer, W.,Esswein, A.,Hofmann, E. (deposition date: 1997-04-09, release date: 1997-10-15, Last modification date: 2021-11-03)

Primary citation

Weidler, M.,Marx, U.C.,Seidel, G.,Schaefer, W.,Hoffmann, E.,Esswein, A.,Roesch, P.
The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution.
Febs Lett., 444:239-244, 1999

PubMed Abstract: 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.

PubMed: 10050767
DOI: 10.1016/S0014-5793(98)01658-5

Experimental method

SOLUTION NMR