Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer (Q27637725)

6

object named as

Erhard Hohenester

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author name string

Oren Bogin

1

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Eran Rom

3

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Josef Singer

4

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Avner Yayon

Immunohistochemical localization of short chain cartilage collagen (type X) in avian tissues

5

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publication date

February 2002

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published in

Structure

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volume

10

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issue

2

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page(s)

165-73

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cites work

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The fibrillar collagens, collagen VIII, collagen X and the C1q complement proteins share a similar domain in their C-terminal non-collagenous regions

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Metaphyseal chondrodysplasia type Schmid mutations are predicted to occur in two distinct three-dimensional clusters within type X collagen NC1 domains that retain the ability to trimerize

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Schmid's metaphyseal chondrodysplasia mutations interfere with folding of the C-terminal domain of human collagen X expressed in Escherichia coli

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The noncollagenous domain 1 of type X collagen. A novel motif for trimer and higher order multimer formation without a triple helix

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Characterization of the collagen in the hexagonal lattice of Descemet's membrane: its relation to type VIII collagen

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Macromolecular organization of chicken type X collagen in vitro

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A type X collagen mutation causes Schmid metaphyseal chondrodysplasia

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Spondylometaphyseal dysplasia in mice carrying a dominant negative mutation in a matrix protein specific for cartilage-to-bone transition

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Normal long bone growth and development in type X collagen-null mice

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Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val mutation in the alpha 1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia

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Site-directed mutagenesis of human type X collagen. Expression of alpha1(X) NC1, NC2, and helical mutations in vitro and in transfected cells

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Interaction of collagen alpha1(X) containing engineered NC1 mutations with normal alpha1(X) in vitro. Implications for the molecular basis of schmid metaphyseal chondrodysplasia

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Folding and assembly of type X collagen mutants that cause metaphyseal chondrodysplasia-type schmid. Evidence for co-assembly of the mutant and wild-type chains and binding to molecular chaperones.

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Aberrant signal peptide cleavage of collagen X in Schmid metaphyseal chondrodysplasia. Implications for the molecular basis of the disease

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A nonsense mutation in the carboxyl-terminal domain of type X collagen causes haploinsufficiency in schmid metaphyseal chondrodysplasia

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