Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume 1208, Issue 2, 19 October 1994, Pages 256-262
Stabilized NMR structure of the hypercalcemia of malignancy peptide PTHrP[Ala-26](1–34) amide
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Interactions of PTH with Receptors and Signaling
2015, The Parathyroids: Basic and Clinical Concepts: Third EditionParathyroid Hormone–Receptor Interactions
2008, Principles of Bone Biology: Volume 1-2, Third EditionRole of amino acid side chains in region 17-31 of parathyroid hormone (PTH) in binding to the PTH receptor
2006, Journal of Biological ChemistryCitation Excerpt :The tertiary structure of receptor-bound PTH has been a matter of some debate, with linear and folded structures supported (4, 35). A folded helix-turn-helix structure for PTH-(1–34) was indeed predicted early on based on modeling and structure-activity data (36), and solution-phase NMR studies of PTH and PTHrP ligands generally reveal mid-region flexibility or a hinge between the N- and C-terminal domains (4, 5, 37, 38). A bend in receptor-bound PTH-(1–34) has more recently been suggested by the cross-linking of both [Bpa11]PTH-(1–34) and [Bpa21]PTH-(1–34) to the same segment (Ala165–Asn176) of the PTHR N domain (39).
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