5ljk: Difference between revisions
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<StructureSection load='5ljk' size='340' side='right'caption='[[5ljk]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5ljk' size='340' side='right'caption='[[5ljk]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ljk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5ljk]] 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=5LJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LJK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5ljk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ljk OCA], [https://pdbe.org/5ljk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ljk RCSB], [https://www.ebi.ac.uk/pdbsum/5ljk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ljk ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RET1_HUMAN RET1_HUMAN] Intracellular transport of retinol. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Berni | [[Category: Berni R]] | ||
[[Category: Menozzi | [[Category: Menozzi I]] | ||
[[Category: Vallese | [[Category: Vallese F]] | ||
[[Category: Zanotti | [[Category: Zanotti G]] | ||
Latest revision as of 21:29, 18 October 2023
Crystal structure of human apo CRBP1Crystal structure of human apo CRBP1
Structural highlights
FunctionRET1_HUMAN Intracellular transport of retinol. Publication Abstract from PubMedFour cellular retinol-binding protein (CRBP) types (CRBP1,2,3,4) are encoded in the human genome. Here, we report on X-ray analyses of human apo- and holo-CRBP1, showing nearly identical structures, at variance with the results of a recent study on the same proteins containing a His-Tag, which appears to be responsible for a destabilizing effect on the apoprotein. The analysis of crystallographic B-factors for our structures indicates that the putative portal region, in particular alpha-helix-II, along with Arg58 and the E-F loop, is the most flexible part of both apo- and holoprotein, consistent with its role in ligand uptake and release. Fluorometric titrations of wild type and mutant forms of apo-CRBP1, coupled with X-ray analyses, provided insight into structural and molecular determinants for the interaction of retinol with CRBP1. An approximately stoichiometric binding of retinol to wild type apo-CRBP1 (Kd approximately 4.5nM), significantly lower binding affinity for both mutants Q108L (Kd approximately 65nM) and K40L (Kd approximately 70nM) and very low binding affinity for the double mutant Q108L/K40L (Kd approximately 250nM) were determined, respectively. Overall, our data indicate that the extensive apolar interactions between the ligand and hydrophobic residues lining the retinol binding cavity are sufficient to keep it in its position bound to CRBP1. However, polar interactions of the retinol hydroxyl end group with Gln108 and Lys40 play a key role to induce a high binding affinity and specificity for the interaction. Structural and molecular determinants affecting the interaction of retinol with human CRBP1.,Menozzi I, Vallese F, Polverini E, Folli C, Berni R, Zanotti G J Struct Biol. 2017 Jan 3. pii: S1047-8477(16)30267-2. doi:, 10.1016/j.jsb.2016.12.012. PMID:28057518[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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