3n3f

Publication Abstract from PubMed

Correct folding of the collagen triple helix requires a self-association step which selects and binds alpha-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 beta-sheets and an alpha-helix. The hydrophobic core of the trimer is devoid of solvent molecules and is shaped by beta-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.

Crystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagens.,Wirz JA, Boudko SP, Lerch TF, Chapman MS, Bachinger HP Matrix Biol. 2010 Oct 12. PMID:20932905^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.