1BQT

THREE-DIMENSIONAL STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR-I (IGF-I) DETERMINED BY 1H-NMR AND DISTANCE GEOMETRY, 6 STRUCTURES

1BQT の概要

• エントリーDOI: 10.2210/pdb1bqt/pdb
• NMR情報: BMRB: 4204
• 分子名称: INSULIN-LIKE GROWTH FACTOR-I (1 entity in total)
• 機能のキーワード: growth factor, insulin
• 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: 7663.75

構造登録者

Sato, A.,Nishimura, S.,Ohkubo, T.,Kyogoku, Y.,Koyama, S.,Kobayashi, M.,Yasuda, T.,Kobayashi, Y. (登録日: 1998-08-18, 公開日: 1999-05-18, 最終更新日: 2024-10-30)

主引用文献

Sato, A.,Nishimura, S.,Ohkubo, T.,Kyogoku, Y.,Koyama, S.,Kobayashi, M.,Yasuda, T.,Kobayashi, Y.
Three-dimensional structure of human insulin-like growth factor-I (IGF-I) determined by 1H-NMR and distance geometry.
Int.J.Pept.Protein Res., 41:433-440, 1993

PubMed Abstract: The three-dimensional structure of human insulin-like growth factor-I has been determined through a combination of NMR measurements and distance geometry calculations. A total of 320 interatomic distance constraints, including 12 related to the disulfide bridges, were used in these calculations. The resulting structure is characterized by the presence of three helical rods corresponding to the sequence regions, Ala8-Cys18, Gly42-Cys48 and Leu54-Cys61. Furthermore, a turn structure and an extended structure exist in the Gly19-Gly22 and Phe23-Asn26 regions, respectively. Neglecting the N- and C-termini, with their expectedly high degree of mobility as well as a fluctuating C-domain, the r.m.s.d. value is 1.9 A for backbone atoms. Those of the three alpha-helical regions are 1.0, 0.9 and 0.8 A, respectively, 1.8 A being that for the total backbone atoms participating in the formation of these three helices, showing the good convergence of their spatial arrangements. The overall structure obtained here shows that the human IGF-I molecule folds into a spatial structure very similar to that of insulin in an aqueous solution.

PubMed: 8391516

実験手法

SOLUTION NMR