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PDBsum entry 6tqk
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Structural protein
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PDB id
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6tqk
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Contents |
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296 a.a.
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144 a.a.
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153 a.a.
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PDB id:
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| Name: |
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Structural protein
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Title:
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Cryo-em of native human uromodulin (umod)/tamm-horsfall protein (thp) filament.
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Structure:
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Uromodulin. Chain: a, b, c. Synonym: tamm-horsfall urinary glycoprotein,thp
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Source:
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Homo sapiens. Human. Organism_taxid: 9606
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Authors:
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A.Stsiapanava,C.Xu,M.Carroni,B.Wu,L.Jovine
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Key ref:
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A.Stsiapanava
et al.
(2020).
Cryo-EM structure of native human uromodulin, a zona pellucida module polymer.
EMBO J,
39,
e106807.
PubMed id:
DOI:
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Date:
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16-Dec-19
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Release date:
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04-Nov-20
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PROCHECK
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Headers
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References
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P07911
(UROM_HUMAN) -
Uromodulin from Homo sapiens
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Seq:
Struc:
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640 a.a.
296 a.a.
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DOI no:
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EMBO J
39:e106807
(2020)
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PubMed id:
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Cryo-EM structure of native human uromodulin, a zona pellucida module polymer.
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A.Stsiapanava,
C.Xu,
M.Brunati,
S.Zamora-Caballero,
C.Schaeffer,
M.Bokhove,
L.Han,
H.Hebert,
M.Carroni,
S.Yasumasu,
L.Rampoldi,
B.Wu,
L.Jovine.
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ABSTRACT
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Assembly of extracellular filaments and matrices mediating fundamental
biological processes such as morphogenesis, hearing, fertilization, and
antibacterial defense is driven by a ubiquitous polymerization module known as
zona pellucida (ZP) "domain". Despite the conservation of this element
from hydra to humans, no detailed information is available on the filamentous
conformation of any ZP module protein. Here, we report a cryo-electron
microscopy study of uromodulin (UMOD)/Tamm-Horsfall protein, the most abundant
protein in human urine and an archetypal ZP module-containing molecule, in its
mature homopolymeric state. UMOD forms a one-start helix with an unprecedented
180-degree twist between subunits enfolded by interdomain linkers that have
completely reorganized as a result of propeptide dissociation. Lateral
interaction between filaments in the urine generates sheets exposing a
checkerboard of binding sites to capture uropathogenic bacteria, and UMOD-based
models of heteromeric vertebrate egg coat filaments identify a common
sperm-binding region at the interface between subunits.
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Links
