3D96

Crystal Structure of the R132K:Y134F Mutant of Apo-Cellular Retinoic Acid Binding Protein Type II at 1.71 Angstroms Resolution

3D96 の概要

• エントリーDOI: 10.2210/pdb3d96/pdb
• 関連するPDBエントリー: 2fr3 2frs 2fs6 2fs7 2g78 2g79 2g7b 3D97 3cwk 3d95
• 分子名称: Cellular retinoic acid-binding protein 2, ACETATE ION (3 entities in total)
• 機能のキーワード: crabpii, retinoic acid, retinoids, beta barrel, high resolution, mutant, nucleus, retinol-binding, transport, vitamin a, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P29373
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31134.62

構造登録者

Vaezeslami, S.,Geiger, J.H. (登録日: 2008-05-26, 公開日: 2008-07-22, 最終更新日: 2024-02-21)

主引用文献

Vaezeslami, S.,Jia, X.,Vasileiou, C.,Borhan, B.,Geiger, J.H.
Structural analysis of site-directed mutants of cellular retinoic acid-binding protein II addresses the relationship between structural integrity and ligand binding.
Acta Crystallogr.,Sect.D, 64:1228-1239, 2008

PubMed Abstract: The structural integrity of cellular retinoic acid-binding protein II (CRABPII) has been investigated using the crystal structures of CRABPII mutants. The overall fold was well maintained by these CRABPII mutants, each of which carried multiple different mutations. A water-mediated network is found to be present across the large binding cavity, extending from Arg111 deep inside the cavity to the alpha2 helix at its entrance. This chain of interactions acts as a ;pillar' that maintains the integrity of the protein. The disruption of the water network upon loss of Arg111 leads to decreased structural integrity of the protein. A water-mediated network can be re-established by introducing the hydrophilic Glu121 inside the cavity, which results in a rigid protein with the alpha2 helix adopting an altered conformation compared with wild-type CRABPII.

PubMed: 19018099
DOI: 10.1107/S0907444908032216

実験手法

X-RAY DIFFRACTION (1.71 Å)