1M3D

Structure of Type IV Collagen NC1 Domains

Summary for 1M3D

• Entry DOI: 10.2210/pdb1m3d/pdb
• Descriptor: Type IV Collagen Noncollagenous Domain- Alpha1, Type IV Collagen Noncollagenous Domain- Alpha2, BROMIDE ION, ... (6 entities in total)
• Functional Keywords: basement membrane, type iv collagen, nc1 domain, network assembly, 3d domain swapping, br-mad, structural protein
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted, extracellular space, extracellular matrix, basement membrane: Q7SIB2 Q7SIB3
• Total number of polymer chains: 12
• Total formula weight: 307846.47

Authors

Sundaramoorthy, M.,Meiyappan, M.,Todd, P.,Hudson, B.G. (deposition date: 2002-06-27, release date: 2003-01-07, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)