1QGM

THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.

1QGM の概要

• エントリーDOI: 10.2210/pdb1qgm/pdb
• NMR情報: BMRB: 4351
• 分子名称: PROTEIN (AMINO-TERMINAL CARP GRANULIN-1) (1 entity in total)
• 機能のキーワード: beta-hairpin stack, conformational stability, cytokine
• 細胞内の位置: Secreted: P81013
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3195.60

構造登録者

Vranken, W.F.,Xu, P.,Ni, F. (登録日: 1999-05-01, 公開日: 1999-12-22, 最終更新日: 2024-11-20)

主引用文献

Vranken, W.F.,Chen, Z.G.,Xu, P.,James, S.,Bennett, H.P.,Ni, F.
A 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein.
J.Pept.Res., 53:590-597, 1999

PubMed Abstract: Upon air oxidation, a peptide corresponding to the 30-residue N-terminal subdomain of carp granulin-1 spontaneously formed the disulfide pairing observed in the native protein. Structural characterization using NMR showed the presence of a defined secondary structure within this peptide. The chemical shifts for most of the alphaCH protons of the peptide and the protein are very similar, and the observed NOE contacts of the peptide strongly resemble those in the protein. A structure calculation of the peptide using NOE distance constraints indicates that the peptide fragment adopts the same conformation as formed within the native protein. The 30-residue N-terminal peptide of carp granulin-1 is the first example of an independently folded stack of two beta-hairpins reinforced by two interhairpin disulfide bonds. Two key areas of the structure show a clustering of hydrophobic residues that may account for its exceptional conformational stability.

PubMed: 10424355
DOI: 10.1034/j.1399-3011.1999.00048.x

実験手法

SOLUTION NMR