1B1V

NMR STRUCTURE OF PSP1, PLASMATOCYTE-SPREADING PEPTIDE FROM PSEUDOPLUSIA INCLUDENS

1B1V の概要

• エントリーDOI: 10.2210/pdb1b1v/pdb
• NMR情報: BMRB: 4292
• 分子名称: PROTEIN (PLASMATOCYTE-SPREADING PEPTIDE) (1 entity in total)
• 機能のキーワード: insect cytokine, plasmatocyte-spreading, egf-like, cytokine
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2511.84

構造登録者

Volkman, B.F.,Clark, K.D.,Anderson, M.E.,Pech, L.L.,Markley, J.L.,Strand, M.R. (登録日: 1998-11-23, 公開日: 1998-12-02, 最終更新日: 2024-10-30)

主引用文献

Volkman, B.F.,Anderson, M.E.,Clark, K.D.,Hayakawa, Y.,Strand, M.R.,Markley, J.L.
Structure of the insect cytokine peptide plasmatocyte-spreading peptide 1 from Pseudoplusia includens.
J.Biol.Chem., 274:4493-4496, 1999

PubMed Abstract: The structure of the recently identified plasmatocyte spreading peptide from the moth Pseudoplusia includens (PSP1) has been determined by NMR spectroscopy. This novel insect cytokine consists of 23 amino acid residues and a single disulfide bond. Torsion angle dynamics calculations utilizing a total of 337 distance constraints yielded an ensemble of 30 structures with an average backbone root mean square deviation for residues 7-22 of 0.18 A from the mean structure. The structure consists of a disordered N-terminal region and a well defined core that is stabilized by numerous hydrophobic interactions and a short beta-hairpin. Structural comparisons confirm that PSP1 adopts an epidermal growth factor (EGF)-like fold with close similarity to the C-terminal subdomain of EGF-like module 5 of human thrombomodulin. The combination of the three-dimensional structure of PSP1 and the extensive literature on EGF-receptor interactions should accelerate the process of identifying the specific residues responsible for receptor binding activity of this family of immunoregulatory peptides.

PubMed: 9988679
DOI: 10.1074/jbc.274.8.4493

実験手法

SOLUTION NMR