7a9y | pdb_00007a9y

Structural comparison of cellular retinoic acid binding protein I and II in the presence and absence of natural and synthetic ligands

spinqualitylabelsall models 7a9y, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7a9y is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.64Å Ligands: GOL, MYR, TDA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RABP1_HUMAN Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors. Publication Abstract from PubMed A detailed understanding of the interactions between small-molecule ligands and their proposed binding targets is of the utmost importance for modern drug-development programs. Cellular retinoic acid-binding proteins I and II (CRABPI and CRABPII) facilitate a number of vital retinoid signalling pathways in mammalian cells and offer a gateway to manipulation of signalling that could potentially reduce phenotypes in serious diseases, including cancer and neurodegeneration. Although structurally very similar, the two proteins possess distinctly different biological functions, with their signalling influence being exerted through both genomic and nongenomic pathways. In this article, crystal structures are presented of the L29C mutant of Homo sapiens CRABPI in complex with naturally occurring fatty acids (1.64 A resolution) and with the synthetic retinoid DC645 (2.41 A resolution), and of CRABPII in complex with the ligands DC479 (1.80 A resolution) and DC645 (1.71 A resolution). DC645 and DC479 are two potential drug compounds identified in a recent synthetic retinoid development program. In particular, DC645 has recently been shown to have disease-modifying capabilities in neurodegenerative disease models by activating both genomic and nongenomic signalling pathways. These co-crystal structures demonstrate a canonical binding behaviour akin to that exhibited with all-trans-retinoic acid and help to explain how the compounds are able to exert an influence on part of the retinoid signalling cascade. Structure-functional relationship of cellular retinoic acid-binding proteins I and II interacting with natural and synthetic ligands.,Tomlinson CWE, Cornish KAS, Whiting A, Pohl E Acta Crystallogr D Struct Biol. 2021 Feb 1;77(Pt 2):164-175. doi: , 10.1107/S2059798320015247. Epub 2021 Feb 5. PMID:33559606 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cellular retinoic acid-binding protein 3D structures

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