3N3F

Crystal Structure of the Human Collagen XV Trimerization Domain: A Potent Trimerizing Unit Common to Multiplexin Collagens

Summary for 3N3F

• Entry DOI: 10.2210/pdb3n3f/pdb
• Descriptor: Collagen alpha-1(XV) chain (2 entities in total)
• Functional Keywords: collagen, extracellular matrix, basement membrane, collagen xv, trimerization domain, folding, association, chain selection, triple helix, multiplexin, collagen xviii, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (By similarity): P39059
• Total number of polymer chains: 2
• Total formula weight: 12518.56

Authors

Wirz, J.A. (deposition date: 2010-05-19, release date: 2010-10-20, Last modification date: 2023-09-06)

Primary citation

Wirz, J.A.,Boudko, S.P.,Lerch, T.F.,Chapman, M.S.,Bachinger, H.P.
Crystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagens.
Matrix Biol., 30:9-15, 2011

PubMed Abstract: Correct folding of the collagen triple helix requires a self-association step which selects and binds α-chains into trimers. Here we report the crystal structure of the trimerization domain of human type XV collagen. The trimerization domain of type XV collagen contains three monomers each composed of four β-sheets and an α-helix. The hydrophobic core of the trimer is devoid of solvent molecules and is shaped by β-sheet planes from each monomer. The trimerization domain is extremely stable and forms at picomolar concentrations. It is found that the trimerization domain of type XV collagen is structurally similar to that of type XVIII, despite only 32% sequence identity. High structural conservation indicates that the multiplexin trimerization domain represents a three dimensional fold that allows for sequence variability while retaining structural integrity necessary for tight and efficient trimerization.

PubMed: 20932905
DOI: 10.1016/j.matbio.2010.09.005

Experimental method

X-RAY DIFFRACTION (2.005 Å)