1GR3

Structure of the human collagen X NC1 trimer

Summary for 1GR3

• Entry DOI: 10.2210/pdb1gr3/pdb
• Descriptor: COLLAGEN X, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: collagen, extracellular matrix, connective tissue
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Secreted, extracellular space, extracellular matrix : Q03692
• Total number of polymer chains: 1
• Total formula weight: 18428.98

Authors

Bogin, O.,Kvansakul, M.,Rom, E.,Singer, J.,Yayon, A.,Hohenester, E. (deposition date: 2001-12-12, release date: 2002-02-14, Last modification date: 2023-12-13)

Primary citation

Bogin, O.,Kvansakul, M.,Rom, E.,Singer, J.,Yayon, A.,Hohenester, E.
Insight Into Schmid Metaphyseal Chondrodysplasia from the Crystal Structure of the Collagen X Nc1 Domain Trimer.
Structure, 10:165-, 2002

PubMed Abstract: Collagen 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.

PubMed: 11839302
DOI: 10.1016/S0969-2126(02)00697-4

Experimental method

X-RAY DIFFRACTION (2 Å)