1ggl
From Proteopedia
(New page: 200px<br /> <applet load="1ggl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggl, resolution 2.31Å" /> '''HUMAN CELLULAR RETI...) |
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| - | [[Image:1ggl.gif|left|200px]]<br /> | + | [[Image:1ggl.gif|left|200px]]<br /><applet load="1ggl" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ggl" size=" | + | |
caption="1ggl, resolution 2.31Å" /> | caption="1ggl, resolution 2.31Å" /> | ||
'''HUMAN CELLULAR RETINOL BINDING PROTEIN III'''<br /> | '''HUMAN CELLULAR RETINOL BINDING PROTEIN III'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two cellular retinol-binding proteins (CRBP I and II) with distinct tissue | + | 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. & 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1GGL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: retinol binding protein]] | [[Category: retinol binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:53 2008'' |
Revision as of 10:49, 21 February 2008
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HUMAN CELLULAR RETINOL BINDING PROTEIN III
Contents |
Overview
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. & 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.
Disease
Known disease associated with this structure: Chondrosarcoma, extraskeletal myxoid OMIM:[601574]
About this Structure
1GGL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Identification, retinoid binding, and x-ray analysis of a human retinol-binding protein., Folli C, Calderone V, Ottonello S, Bolchi A, Zanotti G, Stoppini M, Berni R, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3710-5. PMID:11274389
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