2OQP

Solution structure of human interleukin-21

2OQP の概要

• エントリーDOI: 10.2210/pdb2oqp/pdb
• 分子名称: Interleukin-21 (1 entity in total)
• 機能のキーワード: four helix bundle, cytokine, multiple conformers
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: Q9HBE4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15622.89

構造登録者

Bondensgaard, K.,Breinholt, J. (登録日: 2007-02-01, 公開日: 2007-06-19, 最終更新日: 2024-10-09)

主引用文献

Bondensgaard, K.,Breinholt, J.,Madsen, D.,Omkvist, D.H.,Kang, L.,Worsaae, A.,Becker, P.,Schiodt, C.B.,Hjorth, S.A.
The existence of multiple conformers of interleukin-21 directs engineering of a superpotent analogue.
J.Biol.Chem., 282:23326-23336, 2007

PubMed Abstract: The high resolution three-dimensional structure of human interleukin (hIL)-21 has been resolved by heteronuclear NMR spectroscopy. Overall, the hIL-21 structure is dominated by a well defined central four-helical bundle, arranged in an up-up-down-down topology, as observed for other cytokines. A segment of the hIL-21 molecule that includes the third helical segment, helix C, is observed to exist in two distinct and interchangeable states. In one conformer, the helix C segment is presented in a regular, alpha-helical conformation, whereas in the other conformer, this segment is largely disordered. A structure-based sequence alignment of hIL-21 with receptor complexes of the related cytokines, interleukin-2 and -4, implied that this particular segment is involved in receptor binding. An hIL-21 analog was designed to stabilize the region around helix C through the introduction of a segment grafted from hIL-4. This novel hIL-21 analog was demonstrated to exhibit a 10-fold increase in potency in a cellular assay.

PubMed: 17565991
DOI: 10.1074/jbc.M701313200

実験手法

SOLUTION NMR