1JJX

Solution Structure of Recombinant Human Brain-type Fatty acid Binding Protein

1JJX の概要

• エントリーDOI: 10.2210/pdb1jjx/pdb
• 関連するPDBエントリー: 1FDQ
• NMR情報: BMRB: 5320
• 分子名称: BRAIN-TYPE FATTY ACID BINDING PROTEIN (1 entity in total)
• 機能のキーワード: beta barrel, lipid binding protein, fatty acid carrier, 15n isotope enrichment, nmr spectroscopy
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: O15540
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14776.70

構造登録者

Rademacher, M.,Zimmerman, A.W.,Rueterjans, H.,Veerkamp, J.H.,Luecke, C. (登録日: 2001-07-10, 公開日: 2002-10-30, 最終更新日: 2024-05-22)

主引用文献

Rademacher, M.,Zimmerman, A.W.,Ruterjans, H.,Veerkamp, J.H.,Lucke, C.
Solution structure of fatty acid-binding protein from human brain.
Mol.Cell.Biochem., 239:61-68, 2002

PubMed Abstract: Human brain-type fatty acid-binding protein (B-FABP) has been recombinantly expressed in Escherichia coli both unlabelled and 15N-enriched for structure investigation in solution using high-resolution NMR spectroscopy. The sequential assignments of the 1H and 15N resonances were achieved by applying multidimensional homo- and heteronuclear NMR experiments. The ensemble of the 20 final energy-minimized structures, representing human B-FABP in solution, have been calculated based on a total of 2490 meaningful distance constraints. The overall B-FABP structure exhibits the typical backbone conformation described for other members of the FABP family, consisting often antiparallel beta-strands (betaA to betaJ) that form two almost orthogonal beta-sheets, a helix-turn-helix motif that closes the beta-barrel on one side, and a short N-terminal helical loop. A comparison with the crystal structure of the same protein complexed with docosahexaenoic acid reveals only minor differences in both secondary structure and overall topology. Moreover, the NMR data indicate a close structural relationship between human B-FABP and heart-type FABP with respect to fatty acid binding inside the protein cavity.

PubMed: 12479569
DOI: 10.1023/A:1020566909213

実験手法

SOLUTION NMR