1HTH
The solution structure of cyclic human parathyroid hormone fragment 1-34, NMR, 10 structures
1HTH の概要
| エントリーDOI | 10.2210/pdb1hth/pdb |
| 分子名称 | CYCLIC PARATHYROID HORMONE (1 entity in total) |
| 機能のキーワード | human parathyroid hormone, cyclic, ornithine, norleucine, hormone |
| 由来する生物種 | Homo sapiens (HUMAN) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 4116.70 |
| 構造登録者 | Roesch, P.,Seidel, G.,Schaefer, W.,Esswein, A.,Hofmann, E. (登録日: 1997-04-09, 公開日: 1997-10-15, 最終更新日: 2021-11-03) |
| 主引用文献 | 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 Cited by 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: 10050767DOI: 10.1016/S0014-5793(98)01658-5 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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