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| == Structural highlights == | | == Structural highlights == |
| <scene name='48/488393/Cv/6'>Retinol binds to cellular RBP II inside its internal cavity</scene><ref>PMID:18076076</ref>. <scene name='48/488393/Cv/5'>Active site</scene>. Water molecules shown as red spheres. | | <scene name='48/488393/Cv/7'>Retinol binds to cellular RBP II inside its internal cavity</scene><ref>PMID:18076076</ref>. <scene name='48/488393/Cv/8'>Active site</scene>. Water molecules are shown as red spheres. |
| </StructureSection> | | </StructureSection> |
| ==3D structures of retinol-binding protein== | | ==3D structures of retinol-binding protein== |
Revision as of 13:10, 26 August 2019
| Function
Retinol-binding protein (RBP) are carrier proteins which bind retinol (vitamin A alcohol). Human RBP4 is the carrier of retinol in the blood. It delivers retinol from the liver to the peripheral tissues. RBP also functions in regulation, metabolism and activities of retinoids. Retinol is being protected from oxidation and becomes soluble when bound to RBP. RBP is classified according to its site of activity. Plasma RBP (PRBP) carries retinol in blood[1] while cellular RBP (CRBP) carries retinol in the cell[2].
Relevance
RBP is used to assess vitamin A deficiency as it binds 1:1 to retinol[3]. RBP IV is used as biomarker for renal dysfunction and cardiovascular disease in type II diabetes[4].
Structural highlights
Retinol binds to cellular RBP II inside its internal cavity[5]. Active site. Water molecules are shown as red spheres.
- ↑ Goodman DS. Plasma retinol-binding protein. Ann N Y Acad Sci. 1980;348:378-90. PMID:6994566
- ↑ Ong DE. Cellular retinoid-binding proteins. Arch Dermatol. 1987 Dec;123(12):1693-1695a. PMID:2825608
- ↑ Filteau SM, Willumsen JF, Sullivan K, Simmank K, Gamble M. Use of the retinol-binding protein: transthyretin ratio for assessment of vitamin A status during the acute-phase response. Br J Nutr. 2000 May;83(5):513-20. PMID:10953676
- ↑ Cabre A, Lazaro I, Girona J, Manzanares J, Marimon F, Plana N, Heras M, Masana L. Retinol-binding protein 4 as a plasma biomarker of renal dysfunction and cardiovascular disease in type 2 diabetes. J Intern Med. 2007 Oct;262(4):496-503. PMID:17875187 doi:https://dx.doi.org/10.1111/j.1365-2796.2007.01849.x
- ↑ Tarter M, Capaldi S, Carrizo ME, Ambrosi E, Perduca M, Monaco HL. Crystal structure of human cellular retinol-binding protein II to 1.2 A resolution. Proteins. 2008 Mar;70(4):1626-30. PMID:18076076 doi:https://dx.doi.org/10.1002/prot.21848
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3D structures of retinol-binding protein
Updated on 26-August-2019
{"openlevels":0}
- Plasma retinol-binding protein (PRBP)
- Plasma RBP complex
- 3bsz - hRBP II + transthyretin + antibody + retinol
- 3fmz - hRBP IV + non-retinoid ligand
- 2wq9 - hRBP IV + oleate
- 2wr6 - hRBP IV + linoleate
- 2wqa - hRBP IV + transthyretin + oleate
- 4o9s, 4psq - hRBP IV + non-retinoid
- 1iiu - RBP + retinol – chicken
- 1rlb - cRBP + transthyretin
- 1kt3, 1kt4, 1kt5, 1kt6, 1kt7, 1hbp - RBP + retinol
- 1erb, 1fel, 1fem, 1fen - bRBP + retinol derivative
- 1qab - rRBP + transthyretin
- Cellular RBP (CRBP)
- 1jbh, 1kgl, 1mx7 - rRBP I – rat - NMR
- 5h9a, 5ljb, 5ljc, 5ljg, 5ljk - hRBP I
- 5ljd, 5lje, 5ljh - hRBP I (mutant)
- 1b4m - rRBP II – NMR
- 1opa – rRBP II
- 2rcq, 4zh9 - hRBP II
- 4zgu, 4zh6, 4zr2, 4zcb, 5dg4, 5dpq - hRBP II (mutant)
- 1ggl - hRBP III
- 1lpj, 6at8 - hRBP IV
- 1kqx – ZeRBP – zebrafish
- 4uet - NaRBP – Necator americanus - NMR
- Cellular RBP complex
- 1mx8 - rRBP I + retinol – NMR
- 5h8t, 5hbs - hRBP I + retinol
- 5ha1 - hRBP I + retinol derivative
- 1eii - rRBP II + retinol – NMR
- 2rct, 4qyn, 4qyp, 4qzt, 4qzu - hRBP II + retinol
- 4zj0, 4ruu, 4ede, 4eej, 4efg, 4exz, 4gkc, 5f6b, 5f7g, 5ffh, 5f58, 5faz, 5fen - hRBP II (mutant) + retinol
- 1kqw - ZeRBP + retinol
- 1crb, 1opb - rRBP + retinol
- 4xcp - NaRBP + palmitate
- Nematode and fatty acid RBP
- 4xcp - hhRBP - human hookworm
- 4uet - hhRBP - NMR
References
