1jbh

<StructureSection load='1jbh' size='340' side='right'caption='[[1jbh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1jbh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JBH 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;'>[[1kgl|1kgl]], [[1crb|1crb]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RBP-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>

[[https://www.uniprot.org/uniprot/RET1_RAT RET1_RAT]] Intracellular transport of retinol.

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== Publication Abstract from PubMed ==

Retinoid-binding proteins play an important role in regulating transport, storage, and metabolism of vitamin A and its derivatives. The solution structure and backbone dynamics of rat cellular retinol-binding protein type I (CRBP) in the apo- and holo-form have been determined and compared using multidimensional high resolution NMR spectroscopy. The global fold of the protein is consistent with the common motif described for members of the intracellular lipid-binding protein family. The most relevant difference between the NMR structure ensembles of apo- and holoCRBP is the higher backbone disorder, in the ligand-free form, of some segments that frame the putative entrance to the ligand-binding site. These comprise alpha-helix II, the subsequent linker to beta-strand B, the hairpin turn between beta-strands C and D, and the betaE-betaF turn. The internal backbone dynamics, obtained from 15N relaxation data (T1, T2, and heteronuclear nuclear Overhauser effect) at two different fields, indicate several regions with significantly higher backbone mobility in the apoprotein, including the betaC-betaD and betaE-betaF turns. Although apoCRBP contains a binding cavity more shielded than that of any other retinoid carrier, conformational flexibility in the portal region may assist retinol uptake. The stiffening of the backbone in the holoprotein guarantees the stability of the complex during retinol transport and suggests that targeted retinol release requires a transiently open state that is likely to be promoted by the acceptor or the local environment.

Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution.,Franzoni L, Lucke C, Perez C, Cavazzini D, Rademacher M, Ludwig C, Spisni A, Rossi GL, Ruterjans H J Biol Chem. 2002 Jun 14;277(24):21983-97. Epub 2002 Apr 4. PMID:11934897<ref>PMID:11934897</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jbh" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Cavazzini, D]]

[[Category: Franzoni, L]]

[[Category: Ludwig, C]]

[[Category: Luecke, C]]

[[Category: Perez, C]]

[[Category: Rademacher, M]]

[[Category: Rossi, G L]]

[[Category: Rueterjans, H]]

[[Category: Spisni, A]]

[[Category: Retinoid carrier]]