1ALB

CRYSTAL STRUCTURE OF RECOMBINANT MURINE ADIPOCYTE LIPID-BINDING PROTEIN

1ALB の概要

• エントリーDOI: 10.2210/pdb1alb/pdb
• 分子名称: ADIPOCYTE LIPID-BINDING PROTEIN (2 entities in total)
• 機能のキーワード: lipid-binding protein, lipid binding protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm: P04117
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14539.69

構造登録者

Xu, Z.,Banaszak, L.J. (登録日: 1992-09-03, 公開日: 1993-10-31, 最終更新日: 2024-02-07)

主引用文献

Xu, Z.,Bernlohr, D.A.,Banaszak, L.J.
Crystal structure of recombinant murine adipocyte lipid-binding protein.
Biochemistry, 31:3484-3492, 1992

PubMed Abstract: Adipocyte lipid-binding protein (ALBP) is the adipocyte member of an intracellular hydrophobic ligand-binding protein family. ALBP is phosphorylated by the insulin receptor kinase upon insulin stimulation. The crystal structure of recombinant murine ALBP has been determined and refined to 2.5 A. The final R factor for the model is 0.18 with good canonical properties. Crystalline ALBP has a conformation which is essentially identical to that of intestinal fatty acid binding protein and myelin P2 protein. Although the crystal structure is of the apo- form, a cavity resembling that in other family members is present. It contains a number of bound and implied unbound water molecules and shows no large obvious portal to the external milieu. The cavity of ALBP, which by homology is the ligand-binding site, is formed by both polar and hydrophobic residues among which is tyrosine 19. Y19 is phosphorylated by the insulin receptor kinase as described in the accompanying paper [Buelt, M. K., Xu, Z., Banaszak, L. J., & Bernlohr, D. A. (1992) Biochemistry (following paper in this issue)]. By comparing ALBP with the earlier structural results on intestinal fatty acid binding protein, it is now possible to delineate conserved amino acids which help form the binding site in this family.

PubMed: 1554730
DOI: 10.1021/bi00128a024

実験手法

X-RAY DIFFRACTION (2.5 Å)