4QZT

Crystal Structure of wild type Human Cellular Retinol Binding Protein II (hCRBPII) bound to retinol at 7 KeV beam energy

Summary for 4QZT

• Entry DOI: 10.2210/pdb4qzt/pdb
• Related: 2RCQ 2RCT 4EDE 4EEJ 4EFG 4QZU
• Descriptor: Retinol-binding protein 2, RETINOL, ACETATE ION, ... (4 entities in total)
• Functional Keywords: retinol, human cellular retinol binding protein ii, intracellular lipid binding protein, x-ray flux, x-ray damage, retinal, retinoid chaperones, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P50120
• Total number of polymer chains: 4
• Total formula weight: 63139.84

Authors

Assar, Z.,Geiger, J.H. (deposition date: 2014-07-28, release date: 2014-12-10, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)