1M3D

Structure of Type IV Collagen NC1 Domains

1M3D の概要

• エントリーDOI: 10.2210/pdb1m3d/pdb
• 分子名称: Type IV Collagen Noncollagenous Domain- Alpha1, Type IV Collagen Noncollagenous Domain- Alpha2, BROMIDE ION, ... (6 entities in total)
• 機能のキーワード: basement membrane, type iv collagen, nc1 domain, network assembly, 3d domain swapping, br-mad, structural protein
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space, extracellular matrix, basement membrane: Q7SIB2 Q7SIB3
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 307846.47

構造登録者

Sundaramoorthy, M.,Meiyappan, M.,Todd, P.,Hudson, B.G. (登録日: 2002-06-27, 公開日: 2003-01-07, 最終更新日: 2024-10-16)

主引用文献

Sundaramoorthy, M.,Meiyappan, M.,Todd, P.,Hudson, B.G.
Crystal Structure of NC1 Domains. Structural Basis for Type IV Collagen Assembly in Basement Membranes
J.Biol.Chem., 277:31142-31153, 2002

PubMed Abstract: Type IV collagen, which is present in all metazoan, exists as a family of six homologous alpha(IV) chains, alpha1-alpha6, in mammals. The six chains assemble into three different triple helical protomers and self-associate as three distinct networks. The network underlies all epithelia as a component of basement membranes, which play important roles in cell adhesion, growth, differentiation, tissue repair and molecular ultrafiltration. The specificity of both protomer and network assembly is governed by amino acid sequences of the C-terminal noncollagenous (NC1) domain of each chain. In this study, the structural basis for protomer and network assembly was investigated by determining the crystal structure of the ubiquitous [(alpha1)(2).alpha2](2) NC1 hexamer of bovine lens capsule basement membrane at 2.0 A resolution. The NC1 monomer folds into a novel tertiary structure. The (alpha1)(2).alpha2 trimer is organized through the unique three-dimensional domain swapping interactions. The differences in the primary sequences of the hypervariable region manifest in different secondary structures, which determine the chain specificity at the monomer-monomer interfaces. The trimer-trimer interface is stabilized by the extensive hydrophobic and hydrophilic interactions without a need for disulfide cross-linking.

PubMed: 11970952
DOI: 10.1074/jbc.M201740200

実験手法

X-RAY DIFFRACTION (2 Å)