1VDF

ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN

1VDF の概要

• エントリーDOI: 10.2210/pdb1vdf/pdb
• 分子名称: CARTILAGE OLIGOMERIC MATRIX PROTEIN, CHLORIDE ION (3 entities in total)
• 機能のキーワード: extracellular matrix protein, assembly domain, cartilage, oligomeric matrix protein, glycoprotein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix (By similarity): P35444
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 26531.10

構造登録者

Malashkevich, V.N. (登録日: 1996-09-12, 公開日: 1997-10-08, 最終更新日: 2024-10-23)

主引用文献

Malashkevich, V.N.,Kammerer, R.A.,Efimov, V.P.,Schulthess, T.,Engel, J.
The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?
Science, 274:761-765, 1996

PubMed Abstract: Oligomerization by the formation of alpha-helical bundles is common in many proteins. The crystal structure of a parallel pentameric coiled coil, constituting the oligomerization domain in the cartilage oligomeric matrix protein (COMP), was determined at 2.05 angstroms resolution. The same structure probably occurs in two other extracellular matrix proteins, thrombospondins 3 and 4. Complementary hydrophobic interactions and conserved disulfide bridges between the alpha helices result in a thermostable structure with unusual properties. The long hydrophobic axial pore is filled with water molecules but can also accommodate small apolar groups. An "ion trap" is formed inside the pore by a ring of conserved glutamines, which binds chloride and probably other monatomic anions. The oligomerization domain of COMP has marked similarities with proposed models of the pentameric transmembrane ion channels in phospholamban and the acetylcholine receptor.

PubMed: 8864111
DOI: 10.1126/science.274.5288.761

実験手法

X-RAY DIFFRACTION (2.05 Å)