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PDBsum entry 4ak3
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Structural protein
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PDB id
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4ak3
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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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Crystal structure of human fibrillar procollagen type iii c- propeptide trimer
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Structure:
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Collagen alpha-1(iii) chain. Chain: a. Fragment: cpropeptide, residues 1222-1466. Synonym: procollagen iii. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293t.
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Resolution:
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3.50Å
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R-factor:
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0.285
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R-free:
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0.337
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Authors:
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J.M.Bourhis,N.Mariano,Y.Zhao,K.Harlos,E.Y.Jones,C.Moali,N.Aghajari, D.J.S.Hulmes
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Key ref:
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J.M.Bourhis
et al.
(2012).
Structural basis of fibrillar collagen trimerization and related genetic disorders.
Nat Struct Biol,
19,
1031-1036.
PubMed id:
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Date:
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21-Feb-12
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Release date:
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12-Sep-12
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PROCHECK
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Headers
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References
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P02461
(CO3A1_HUMAN) -
Collagen alpha-1(III) chain from Homo sapiens
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Seq:
Struc:
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1466 a.a.
227 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 2 residue positions (black
crosses)
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Nat Struct Biol
19:1031-1036
(2012)
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PubMed id:
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Structural basis of fibrillar collagen trimerization and related genetic disorders.
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J.M.Bourhis,
N.Mariano,
Y.Zhao,
K.Harlos,
J.Y.Exposito,
E.Y.Jones,
C.Moali,
N.Aghajari,
D.J.Hulmes.
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ABSTRACT
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The C propeptides of fibrillar procollagens have crucial roles in tissue growth
and repair by controlling both the intracellular assembly of procollagen
molecules and the extracellular assembly of collagen fibrils. Mutations in C
propeptides are associated with several, often lethal, genetic disorders
affecting bone, cartilage, blood vessels and skin. Here we report the crystal
structure of a C-propeptide domain from human procollagen III. It reveals an
exquisite structural mechanism of chain recognition during intracellular
trimerization of the procollagen molecule. It also gives insights into why some
types of collagen consist of three identical polypeptide chains, whereas others
do not. Finally, the data show striking correlations between the sites of
numerous disease-related mutations in different C-propeptide domains and the
degree of phenotype severity. The results have broad implications for
understanding genetic disorders of connective tissues and designing new
therapeutic strategies.
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Links
