Cellular retinoic acid-binding protein: Difference between revisions
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<StructureSection load='' size=' | <StructureSection load='' size='350' side='right' scene='CRABP_I_(_Cellular_Retinoic_Acid_Binding_Protein_)/1cbs_molecularplayground/20' caption='Cellular retinoic acid binding protein I (CRABP I) [[1cbs]]'> | ||
One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
<scene name='CRABP_I_(_Cellular_Retinoic_Acid_Binding_Protein_)/1cbs_molecularplayground/20'>Molecular Playground: CRABP I</scene> | <scene name='CRABP_I_(_Cellular_Retinoic_Acid_Binding_Protein_)/1cbs_molecularplayground/20'>Molecular Playground: CRABP I</scene> | ||
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Molecular Playground banner: CRABP I, a carrier protein for retinoic acid, has an important role for vision. | Molecular Playground banner: CRABP I, a carrier protein for retinoic acid, has an important role for vision. | ||
__TOC__ | |||
==Function== | |||
'''Cellular Retinoic Acid Binding Proteins''' ('''CRABPs''') are small intracellular proteins (15.5 | '''Cellular Retinoic Acid Binding Proteins''' ('''CRABPs''') are small intracellular proteins (15.5 | ||
kDa) that belong to the family of intracellular lipid binding proteins (iLBP) which bind | kDa) that belong to the family of intracellular lipid binding proteins (iLBP) which bind | ||
small hydrophobic ligands. There are two types of CRABPs, CRABP I and CRABP II. They seem to play a role in controlling Retinoic Acid(RA)-mediated differentiation and proliferation processes [http://www.ncbi.nlm.nih.gov/pubmed/8756459?dopt=Abstract/]. During embryonic development, the spatial and temporal expression of the CRABP gene appears to be strictly regulated [http://www.ncbi.nlm.nih.gov/pubmed/2547683]. Therefore, it has been suggested that CRABP could be involved in the formation of gradients of RA across various developing tissues. Although the structure of CRABP I is similar to the cellular retinol-binding proteins, it binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. '''Epididymal RABP (ERABP)''' is an androgen-dependent RABP present in the lumen of the epididymis believed to be involved in sperm maturation. ERABP binds specifically all-trans- and 9-cis-RA. | small hydrophobic ligands. There are two types of CRABPs, CRABP I and CRABP II. They seem to play a role in controlling Retinoic Acid(RA)-mediated differentiation and proliferation processes [http://www.ncbi.nlm.nih.gov/pubmed/8756459?dopt=Abstract/]. During embryonic development, the spatial and temporal expression of the CRABP gene appears to be strictly regulated [http://www.ncbi.nlm.nih.gov/pubmed/2547683]. Therefore, it has been suggested that CRABP could be involved in the formation of gradients of RA across various developing tissues. Although the structure of CRABP I is similar to the cellular retinol-binding proteins, it binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. '''Epididymal RABP (ERABP)''' is an androgen-dependent RABP present in the lumen of the epididymis believed to be involved in sperm maturation. ERABP binds specifically all-trans- and 9-cis-RA. | ||
*'''CRABP I''' is expressed during embryogenesis and also in adult tissues. | |||
*'''CRABP II''' is expressed in skin embryogenesis. | |||
*'''CRABP IV''' promotes oxidative stress by decreasing endothelial mitochondrial function. | |||
==Structure== | ==Structure== | ||
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of CRABPs is proposed to occur via a region of the protein comprising determinants | of CRABPs is proposed to occur via a region of the protein comprising determinants | ||
from the βC-D loop, the βE-F loop and the N-terminal region of helix II. This region of the protein referred to as the “portal” region of the protein has been extensively studied in other members of the iLBP family, in particular in the fatty acid binding protein, by X-ray crystallography, mutational analysis and multidimensional NMR [http://pubs.acs.org/doi/abs/10.1021/bi961890r]. | from the βC-D loop, the βE-F loop and the N-terminal region of helix II. This region of the protein referred to as the “portal” region of the protein has been extensively studied in other members of the iLBP family, in particular in the fatty acid binding protein, by X-ray crystallography, mutational analysis and multidimensional NMR [http://pubs.acs.org/doi/abs/10.1021/bi961890r]. | ||
==3D structure of cellular retinoic acid-binding protein== | |||
[[Cellular retinoic acid-binding protein 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
==See Also== | ==See Also== | ||
* [http://en.wikipedia.org/wiki/CRABP1 Cellular retinoic acid-binding protein 1 at Wikipedia] | * [http://en.wikipedia.org/wiki/CRABP1 Cellular retinoic acid-binding protein 1 at Wikipedia] | ||
==References== | ==References== | ||