4QYN

The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinol

4QYN の概要

• エントリーDOI: 10.2210/pdb4qyn/pdb
• 関連するPDBエントリー: 4QYN
• 分子名称: Retinol-binding protein 2, RETINOL, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: beta barrel, transfer protein, kidney, lover, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P50120
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31826.85

構造登録者

Nossoni, Z.,Assar, Z.,Yapici, I.,Nosrati, M.,Wang, W.,Berbasova, T.,Vasileiou, C.,Borhan, B.,Geiger, H. (登録日: 2014-07-24, 公開日: 2014-12-31, 最終更新日: 2024-02-28)

主引用文献

Nossoni, Z.,Assar, Z.,Yapici, I.,Nosrati, M.,Wang, W.,Berbasova, T.,Vasileiou, C.,Borhan, B.,Geiger, J.
Structures of holo wild-type human cellular retinol-binding protein II (hCRBPII) bound to retinol and retinal.
Acta Crystallogr.,Sect.D, 70:3226-3232, 2014

PubMed Abstract: Cellular retinol-binding proteins (CRBPs) I and II, which are members of the intracellular lipid-binding protein (iLBP) family, are retinoid chaperones that are responsible for the intracellular transport and delivery of both retinol and retinal. Although structures of retinol-bound CRBPI and CRBPII are known, no structure of a retinal-bound CRBP has been reported. In addition, the retinol-bound human CRBPII (hCRBPII) structure shows partial occupancy of a noncanonical conformation of retinol in the binding pocket. Here, the structure of retinal-bound hCRBPII and the structure of retinol-bound hCRBPII with retinol fully occupying the binding pocket are reported. It is further shown that the retinoid derivative seen in both the zebrafish CRBP and the hCRBPII structures is likely to be the product of flux-dependent and wavelength-dependent X-ray damage during data collection. The structures of retinoid-bound CRBPs are compared and contrasted, and rationales for the differences in binding affinities for retinal and retinol are provided.

PubMed: 25478840
DOI: 10.1107/S1399004714023839

実験手法

X-RAY DIFFRACTION (1.19 Å)