Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold.
Collagens contain a unique triple-helical structure with a repeating sequence -G-X-Y-, where proline and hydroxyproline are major constituents in X and Y positions, respectively. Folding of the collagen triple helix requires trimerization domains. Once trimerized, collagen chains are correctly aligned and the folding of the triple helix proceeds in a zipper-like fashion. Here we report the isolation, characterization, and crystal structure of the trimerization domain of human type XVIII collagen, a member of the multiplexin family. This domain differs from all other known trimerization domains in other collagens and exhibits a high trimerization potential at picomolar concentrations. Strong chain association and high specificity of binding are needed for multiplexins, which are present at very low levels.
Boudko
Sergei P
SP
Research Department of Shriners Hospital for Children, Portland, OR 97239, USA.
Sasaki
Takako
T
Engel
Jürgen
J
Lerch
Thomas F
TF
Nix
Jay
J
Chapman
Michael S
MS
Bächinger
Hans Peter
HP
D000595:Amino Acid Sequence; D000818:Animals; D043170:Collagen Type XVIII / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D043170:Collagen Type XVIII; D011993:Recombinant Fusion Proteins