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| | <StructureSection load='1lpj' size='340' side='right'caption='[[1lpj]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1lpj' size='340' side='right'caption='[[1lpj]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1lpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LPJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1lpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LPJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1crb|1crb]], [[1opa|1opa]], [[1opb|1opb]], [[1ggl|1ggl]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpj OCA], [https://pdbe.org/1lpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lpj RCSB], [https://www.ebi.ac.uk/pdbsum/1lpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpj ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpj OCA], [https://pdbe.org/1lpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lpj RCSB], [https://www.ebi.ac.uk/pdbsum/1lpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RET7_HUMAN RET7_HUMAN]] Intracellular transport of retinol.
| + | [https://www.uniprot.org/uniprot/RET7_HUMAN RET7_HUMAN] Intracellular transport of retinol. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Berni, R]] | + | [[Category: Berni R]] |
| - | [[Category: Calderone, V]] | + | [[Category: Calderone V]] |
| - | [[Category: Folli, C]] | + | [[Category: Folli C]] |
| - | [[Category: Zanotti, G]] | + | [[Category: Zanotti G]] |
| - | [[Category: Cellular retinol-binding protein]]
| + | |
| - | [[Category: Crbp]]
| + | |
| - | [[Category: Ilbp]]
| + | |
| - | [[Category: Retinol]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Vitamin some]]
| + | |
| Structural highlights
Function
RET7_HUMAN Intracellular transport of retinol.
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
Three cellular retinol-binding protein (CRBP) types (CRBP I, II, and III) with distinct tissue distributions and retinoid binding properties have been structurally characterized thus far. A human binding protein, whose mRNA is expressed primarily in kidney, heart, and transverse colon, is shown here to be a CRBP family member (human CRBP IV), according to amino acid sequence, phylogenetic analysis, gene structure organization, and x-ray structural analysis. Retinol binding to CRBP IV leads to an absorption spectrum distinct from a typical holo-CRBP spectrum and is characterized by an affinity (K(d) = approximately 200 nm) lower than those for CRBP I, II, and III, as established in direct and competitive binding assays. As revealed by mutagenic analysis, the presence in CRBP IV of His(108) in place of Gln(108) is not responsible for the unusual holo-CRBP IV spectrum. The 2-A resolution crystal structure of human apo-CRBP IV is very similar to those of other structurally characterized CRBPs. The side chain of Tyr(60) is present within the binding cavity of the apoprotein and might affect the interaction with the retinol molecule. These results indicate that human CRBP IV belongs to a clearly distinct CRBP subfamily and suggest a relatively different mode of retinol binding for this binding protein.
Ligand binding and structural analysis of a human putative cellular retinol-binding protein.,Folli C, Calderone V, Ramazzina I, Zanotti G, Berni R J Biol Chem. 2002 Nov 1;277(44):41970-7. Epub 2002 Aug 9. PMID:12177003[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Folli C, Calderone V, Ramazzina I, Zanotti G, Berni R. Ligand binding and structural analysis of a human putative cellular retinol-binding protein. J Biol Chem. 2002 Nov 1;277(44):41970-7. Epub 2002 Aug 9. PMID:12177003 doi:10.1074/jbc.M207124200
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