1JJJ

SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN

1JJJ の概要

• エントリーDOI: 10.2210/pdb1jjj/pdb
• 関連するPDBエントリー: 1B56
• NMR情報: BMRB: 5083
• 分子名称: EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN (E-FABP) (1 entity in total)
• 機能のキーワード: beta barrel, fatty acid carrier, holo form, nmr spectroscopy, 15n isotope enrichment, lipid binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q01469
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15185.46

構造登録者

Gutierrez-Gonzalez, L.H.,Ludwig, C.,Hohoff, C.,Rademacher, M.,Hanhoff, T.,Rueterjans, H.,Spener, F.,Luecke, C. (登録日: 2001-07-06, 公開日: 2002-06-19, 最終更新日: 2024-11-06)

主引用文献

Gutierrez-Gonzalez, L.H.,Ludwig, C.,Hohoff, C.,Rademacher, M.,Hanhoff, T.,Rueterjans, H.,Spener, F.,Luecke, C.
Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP)
BIOCHEM.J., 364:725-737, 2002

PubMed Abstract: Human epidermal-type fatty acid-binding protein (E-FABP) belongs to a family of intracellular 14-15 kDa lipid-binding proteins, whose functions have been associated with fatty acid signalling, cell growth, regulation and differentiation. As a contribution to understanding the structure-function relationship, we report in the present study features of its solution structure and backbone dynamics determined by NMR spectroscopy. Applying multi-dimensional high-resolution NMR techniques on unlabelled and 15N-enriched recombinant human E-FABP, the 1H and 15N resonance assignments were completed. On the basis of 2008 distance restraints, the three-dimensional solution structure of human E-FABP was subsequently obtained (backbone atom root-mean-square deviation of 0.92+/-0.11 A; where 1 A=0.1 nm), consisting mainly of 10 anti-parallel beta-strands that form a beta-barrel structure. 15N relaxation experiments (T1, T2 and heteronuclear nuclear Overhauser effects) at 500, 600 and 800 MHz provided information on the internal dynamics of the protein backbone. Nearly all non-terminal backbone amide groups showed order parameters S(2)>0.8, with an average value of 0.88+/-0.04, suggesting a uniformly low backbone mobility in the nanosecond-to-picosecond time range. Moreover, hydrogen/deuterium exchange experiments indicated a direct correlation between the stability of the hydrogen-bonding network in the beta-sheet structure and the conformational exchange in the millisecond-to-microsecond time range. The features of E-FABP backbone dynamics elaborated in the present study differ markedly from those of the phylogenetically closely related heart-type FABP and the more distantly related ileal lipid-binding protein, implying a strong interdependence with the overall protein stability and possibly also with the ligand-binding affinity for members of the lipid-binding protein family.

PubMed: 12049637
DOI: 10.1042/BJ20020039

実験手法

SOLUTION NMR