 |
PDBsum entry 4ak3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Structural protein
|
PDB id
|
|
|
|
4ak3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis of fibrillar collagen trimerization and related genetic disorders.
|
|
|
Authors
|
|
J.M.Bourhis,
N.Mariano,
Y.Zhao,
K.Harlos,
J.Y.Exposito,
E.Y.Jones,
C.Moali,
N.Aghajari,
D.J.Hulmes.
|
|
|
Ref.
|
|
Nat Struct Biol, 2012,
19,
1031-1036.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Production and crystallization of the c-Propeptide trimer from human procollagen III.
|
|
|
Authors
|
|
J.M.Bourhis,
N.Mariano,
Y.Zhao,
T.S.Walter,
K.El omari,
F.Delolme,
C.Moali,
D.J.Hulmes,
N.Aghajari.
|
|
|
Ref.
|
|
Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012,
68,
1209-1213.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
