HUMAN CELLULAR RETINOL BINDING PROTEIN IIIHUMAN CELLULAR RETINOL BINDING PROTEIN III

Structural highlights

1ggl 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 2.31Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RET5_HUMAN Intracellular transport of retinol.[1]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Folli C, Calderone V, Ottonello S, Bolchi A, Zanotti G, Stoppini M, Berni R. Identification, retinoid binding, and x-ray analysis of a human retinol-binding protein. Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3710-5. PMID:11274389 doi:http://dx.doi.org/10.1073/pnas.061455898
  2. Folli C, Calderone V, Ottonello S, Bolchi A, Zanotti G, Stoppini M, Berni R. Identification, retinoid binding, and x-ray analysis of a human retinol-binding protein. Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3710-5. PMID:11274389 doi:http://dx.doi.org/10.1073/pnas.061455898

1ggl, resolution 2.31Å

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