1GR3

Structure of the human collagen X NC1 trimer

1GR3 の概要

• エントリーDOI: 10.2210/pdb1gr3/pdb
• 分子名称: COLLAGEN X, 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: collagen, extracellular matrix, connective tissue
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix : Q03692
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18428.98

構造登録者

Bogin, O.,Kvansakul, M.,Rom, E.,Singer, J.,Yayon, A.,Hohenester, E. (登録日: 2001-12-12, 公開日: 2002-02-14, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)