1GL4

Nidogen-1 G2/Perlecan IG3 Complex

Summary for 1GL4

• Entry DOI: 10.2210/pdb1gl4/pdb
• Related: 1H4U
• Descriptor: NIDOGEN-1, BASEMENT MEMBRANE-SPECIFIC HEPARAN SULFATE PROTEOGLYCAN CORE PROTEIN, ZINC ION, ... (5 entities in total)
• Functional Keywords: basement membrane, immunoglobulin-like domain, extracellular matrix, proteoglycan, heparan sulfate
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Secreted, extracellular space, extracellular matrix, basement membrane: P10493 1GL4
• Total number of polymer chains: 2
• Total formula weight: 42216.73

Authors

Kvansakul, M.,Hopf, M.,Ries, A.,Timpl, R.,Hohenester, E. (deposition date: 2001-08-23, release date: 2001-11-28, Last modification date: 2024-10-23)

Primary citation

Kvansakul, M.,Hopf, M.,Ries, A.,Timpl, R.,Hohenester, E.
Structural Basis for the High-Affinity Interaction of Nidogen-1 with Immunoglobulin-Like Domain 3 of Perlecan
Embo J., 20:5342-, 2001

PubMed Abstract: Nidogen and perlecan are large multifunctional basement membrane (BM) proteins conserved in all metazoa. Their high-affinity interaction, which is likely to contribute to BM assembly and function, is mediated by the central G2 domain in nidogen and the third immunoglobulin (IG)-like domain in perlecan, IG3. We have solved the crystal structure at 2.0 A resolution of the mouse nidogen-1 G2-perlecan IG3 complex. Perlecan IG3 belongs to the I-set of the IG superfamily and binds to the wall of the nidogen-1 G2 beta-barrel using beta-strands C, D and F. Nidogen-1 residues participating in the extensive interface are highly conserved, whereas the corresponding binding site on perlecan is more variable. We hypothesize that a second, as yet unidentified, activity of nidogen overlaps with perlecan binding and accounts for the unusually high degree of surface conservation in the G2 domain.

PubMed: 11574465
DOI: 10.1093/EMBOJ/20.19.5342

Experimental method

X-RAY DIFFRACTION (2 Å)