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PDBsum entry 4zj0
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Transport protein
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PDB id
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4zj0
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PDB id:
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| Name: |
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Transport protein
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Title:
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The crystal structure of monomer q108k:k40l:y60w crbpii bound to all- trans-retinal
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Structure:
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Retinol-binding protein 2. Chain: a, b. Fragment: unp residues 2-134. Synonym: cellular retinol-binding protein ii,crbp-ii. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: rbp2, crbp2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.50Å
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R-factor:
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0.201
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R-free:
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0.251
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Authors:
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Z.Nossoni,Z.Assar,W.Wang,C.Vasileiou,B.Borhan,J.H.Geiger
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Key ref:
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Z.Assar
et al.
(2016).
Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.
Structure,
24,
1590-1598.
PubMed id:
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Date:
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28-Apr-15
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Release date:
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11-May-16
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PROCHECK
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Headers
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References
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P50120
(RET2_HUMAN) -
Retinol-binding protein 2 from Homo sapiens
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Seq:
Struc:
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134 a.a.
133 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Structure
24:1590-1598
(2016)
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PubMed id:
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Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.
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Z.Assar,
Z.Nossoni,
W.Wang,
E.M.Santos,
K.Kramer,
C.McCornack,
C.Vasileiou,
B.Borhan,
J.H.Geiger.
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ABSTRACT
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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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