4zr2: Difference between revisions
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==Crystal Structure of the Domain-Swapped Dimer K40L:Q108K:Y60W mutant of Human Cellular Retinol Binding Protein II== | ==Crystal Structure of the Domain-Swapped Dimer K40L:Q108K:Y60W mutant of Human Cellular Retinol Binding Protein II== | ||
<StructureSection load='4zr2' size='340' side='right' caption='[[4zr2]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4zr2' size='340' side='right'caption='[[4zr2]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zr2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZR2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4zr2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZR2 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4zr2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4zr2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Assar, Z]] | [[Category: Assar, Z]] | ||
[[Category: Geiger, J H]] | [[Category: Geiger, J H]] | ||
Revision as of 14:01, 25 December 2019
Crystal Structure of the Domain-Swapped Dimer K40L:Q108K:Y60W mutant of Human Cellular Retinol Binding Protein IICrystal Structure of the Domain-Swapped Dimer K40L:Q108K:Y60W mutant of Human Cellular Retinol Binding Protein II
Structural highlights
Function[RET2_HUMAN] Intracellular transport of retinol. Publication Abstract from PubMedHuman 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. Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.,Assar Z, Nossoni Z, Wang W, Santos EM, Kramer K, McCornack C, Vasileiou C, Borhan B, Geiger JH Structure. 2016 Sep 6;24(9):1590-8. doi: 10.1016/j.str.2016.05.022. Epub 2016 Aug, 11. PMID:27524203[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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