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PDBsum entry 5ik7
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Structural protein
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PDB id
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5ik7
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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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Laminin a2lg45 i-form, apo.
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Structure:
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Laminin subunit alpha-2. Chain: a, b. Synonym: laminin m chain,laminin-12 subunit alpha,laminin-2 subunit alpha,laminin-4 subunit alpha,merosin heavy chain. Engineered: yes
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: lama2. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293
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Resolution:
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2.00Å
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R-factor:
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0.190
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R-free:
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0.219
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Authors:
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D.C.Briggs,E.Hohenester,K.P.Campbell
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Key ref:
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D.C.Briggs
et al.
(2016).
Structural basis of laminin binding to the LARGE glycans on dystroglycan.
Nat Chem Biol,
12,
810-814.
PubMed id:
DOI:
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Date:
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03-Mar-16
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Release date:
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10-Aug-16
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PROCHECK
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Headers
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References
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Q60675
(LAMA2_MOUSE) -
Laminin subunit alpha-2 from Mus musculus
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Seq:
Struc:
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3118 a.a.
381 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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DOI no:
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Nat Chem Biol
12:810-814
(2016)
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PubMed id:
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Structural basis of laminin binding to the LARGE glycans on dystroglycan.
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D.C.Briggs,
T.Yoshida-Moriguchi,
T.Zheng,
D.Venzke,
M.E.Anderson,
A.Strazzulli,
M.Moracci,
L.Yu,
E.Hohenester,
K.P.Campbell.
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ABSTRACT
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Dystroglycan is a highly glycosylated extracellular matrix receptor with
essential functions in skeletal muscle and the nervous system. Reduced matrix
binding by α-dystroglycan (α-DG) due to perturbed glycosylation is a
pathological feature of several forms of muscular dystrophy.
Like-acetylglucosaminyltransferase (LARGE) synthesizes the matrix-binding
heteropolysaccharide [-glucuronic acid-β1,3-xylose-α1,3-]n. Using a dual
exoglycosidase digestion, we confirm that this polysaccharide is present on
native α-DG from skeletal muscle. The atomic details of matrix binding were
revealed by a high-resolution crystal structure of laminin-G-like (LG) domains 4
and 5 (LG4 and LG5) of laminin-α2 bound to a LARGE-synthesized oligosaccharide.
A single glucuronic acid-β1,3-xylose disaccharide repeat straddles a Ca(2+) ion
in the LG4 domain, with oxygen atoms from both sugars replacing Ca(2+)-bound
water molecules. The chelating binding mode accounts for the high affinity of
this protein-carbohydrate interaction. These results reveal a previously
uncharacterized mechanism of carbohydrate recognition and provide a structural
framework for elucidating the mechanisms underlying muscular dystrophy.
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Links
