1gr3
From Proteopedia
Structure of the human collagen X NC1 trimer
Structural highlights
DiseaseCOAA1_HUMAN Defects in COL10A1 are the cause of Schmid type metaphyseal chondrodysplasia (SMCD) [MIM:156500. SMCD is a dominantly inherited disorder of the osseous skeleton. The cardinal features of the phenotype are mild short stature, coxa vara and a waddling gait. Radiography usually shows sclerosis of the ribs, flaring of the metaphyses, and a wide irregular growth plate, especially of the knees. A variant form of SMCD is spondylometaphyseal dysplasia Japanese type. It is characterized by spinal involvement comprising mild platyspondyly, vertebral body abnormalities, and end-plate irregularity.[1] [2] [3] [4] [5] [6] [7] [8] FunctionCOAA1_HUMAN Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage. Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCollagen X is expressed specifically in the growth plate of long bones. Its C1q-like C-terminal NC1 domain forms a stable homotrimer and is crucial for collagen X assembly. Mutations in the NC1 domain cause Schmid metaphyseal chondrodysplasia (SMCD). The crystal structure at 2.0 A resolution of the human collagen X NC1 domain reveals an intimate trimeric assembly strengthened by a buried cluster of calcium ions. Three strips of exposed aromatic residues on the surface of NC1 trimer are likely to be involved in the supramolecular assembly of collagen X. Most internal SMCD mutations probably prevent protein folding, whereas mutations of surface residues may affect the collagen X suprastructure in a dominant-negative manner. Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer.,Bogin O, Kvansakul M, Rom E, Singer J, Yayon A, Hohenester E Structure. 2002 Feb;10(2):165-73. PMID:11839302[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Large Structures | Bogin O | Hohenester E | Kvansakul M | Rom E | Singer J | Yayon A