1ggl: Difference between revisions

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{{Seed}}
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{{STRUCTURE_1ggl|  PDB=1ggl  |  SCENE=  }}  
{{STRUCTURE_1ggl|  PDB=1ggl  |  SCENE=  }}  


'''HUMAN CELLULAR RETINOL BINDING PROTEIN III'''
===HUMAN CELLULAR RETINOL BINDING PROTEIN III===




==Overview==
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Two cellular retinol-binding proteins (CRBP I and II) with distinct tissue distributions and retinoid-binding properties have been recognized thus far in mammals. Here, we report the identification of a human retinol-binding protein resembling type I (55.6% identity) and type II (49.6% identity) CRBPs, but with a unique H residue in the retinoid-binding site and a distinctively different tissue distribution. Additionally, this binding protein (CRBP III) exhibits a remarkable sequence identity (62.2%) with the recently identified iota-crystallin/CRBP of the diurnal gecko Lygodactylus picturatus [Werten, P. J. L., Roll, B., van Alten, D. M. F. &amp; de Jong, W. W. (2000) Proc. Natl. Acad. Sci. USA 97, 3282-3287 (First Published March 21, 2000; 10.1073/pnas.050500597)]. CRBP III and all-trans-retinol form a complex (K(d) approximately 60 nM), the absorption spectrum of which is characterized by the peculiar fine structure typical of the spectra of holo-CRBP I and II. As revealed by a 2.3-A x-ray molecular model of apo-CRBP III, the amino acid residues that line the retinol-binding site in CRBP I and II are positioned nearly identically in the structure of CRBP III. At variance with the human CRBP I and II mRNAs, which are most abundant in ovary and intestine, respectively, the CRBP III mRNA is expressed at the highest levels in kidney and liver thus suggesting a prominent role for human CRBP III as an intracellular mediator of retinol metabolism in these tissues.
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{{ABSTRACT_PUBMED_11274389}}


==About this Structure==
==About this Structure==
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[[Category: Carrier]]
[[Category: Carrier]]
[[Category: Retinol binding protein]]
[[Category: Retinol binding protein]]
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