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PDBsum entry 5fww
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Signaling protein
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PDB id
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5fww
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Contents |
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612 a.a.
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288 a.a.
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76 a.a.
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PDB id:
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| Name: |
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Signaling protein
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Title:
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Wnt modulator kremen in complex with dkk1 (crd2) and lrp6 (pe3pe4)
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Structure:
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Low-density lipoprotein receptor-related protein 6. Chain: a. Fragment: pe3pe4, residues 630-1246. Synonym: lrp-6. Engineered: yes. Kremen protein 1. Chain: b. Fragment: ecd, residues 30-322. Synonym: dickkopf receptor, kringle domain-containing transmembrane
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: lrp6. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293. Gene: kremen1, kremen, krm1. Gene: dkk1, unq492/pro1008.
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Resolution:
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3.50Å
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R-factor:
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0.323
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R-free:
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0.355
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Authors:
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M.Zebisch,V.A.Jackson,E.Y.Jones
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Key ref:
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M.Zebisch
et al.
(2016).
Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf.
Structure,
24,
1599-1605.
PubMed id:
DOI:
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Date:
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21-Feb-16
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Release date:
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20-Jul-16
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PROCHECK
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Headers
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References
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O75581
(LRP6_HUMAN) -
Low-density lipoprotein receptor-related protein 6 from Homo sapiens
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Seq:
Struc:
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1613 a.a.
612 a.a.*
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DOI no:
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Structure
24:1599-1605
(2016)
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PubMed id:
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Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf.
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M.Zebisch,
V.A.Jackson,
Y.Zhao,
E.Y.Jones.
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ABSTRACT
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Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins,
hallmark secreted antagonists of canonical Wnt signaling. We present here three
crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions
between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight
interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB
structural domains. The structures reveal an unpredicted homology of the WSC
domain to hepatocyte growth factor. We further report the general architecture
of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm,
determined from a low-resolution complex crystal structure between
β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4),
the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. DKK1CRD2 is sandwiched
between LRP6PE3 and KRM1Kringle-WSC. Modeling studies supported by surface
plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.
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Links
