5dpq

<StructureSection load='5dpq' size='340' side='right' caption='[[5dpq]], [[Resolution|resolution]] 1.77&Aring;' scene=''>

<table><tr><td colspan='2'>[[5dpq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DPQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DPQ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dpq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dpq OCA], [http://pdbe.org/5dpq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dpq RCSB], [http://www.ebi.ac.uk/pdbsum/5dpq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dpq ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RET2_HUMAN RET2_HUMAN]] Intracellular transport of retinol.

Human Cellular Retinol Binding Protein II (hCRBPII), a member of the intracellular lipid-binding protein family, is a monomeric protein responsible for the intracellular transport of retinol and retinal. Herein we report that hCRBPII forms an extensive domain-swapped dimer during bacterial expression. The domain-swapped region encompasses almost half of the protein. The dimer represents a novel structural architecture with the mouths of the two binding cavities facing each other, producing a new binding cavity that spans the length of the protein complex. Although wild-type hCRBPII forms the dimer, the propensity for dimerization can be substantially increased via mutation at Tyr60. The monomeric form of the wild-type protein represents the thermodynamically more stable species, making the domain-swapped dimer a kinetically trapped entity. Hypothetically, the wild-type protein has evolved to minimize dimerization of the folding intermediate through a critical hydrogen bond (Tyr60-Glu72) that disfavors the dimeric form.

 

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== References ==

[[Category: Assar, Z]]

[[Category: Borhan, B]]

[[Category: Geiger, J H]]

[[Category: Nossoni, Z]]

[[Category: Wang, W]]

[[Category: Domain swapped dimer]]

[[Category: Ilbp]]

[[Category: Retinol binding protein]]