TY - JOUR
T1 - Crystal Structure of Human Collagen XVIII Trimerization Domain
T2 - A Novel Collagen Trimerization Fold
AU - Boudko, Sergei P.
AU - Sasaki, Takako
AU - Engel, Jürgen
AU - Lerch, Thomas F.
AU - Nix, Jay
AU - Chapman, Michael S.
AU - Bächinger, Hans Peter
N1 - Funding Information:
Part of this research was performed at the Advanced Light Source, which is supported by the Director, Office of Science, Office of Basic Energy Sciences, Materials Sciences Division, U.S. Department of Energy, under contract no. DE-AC03-76SF00098, at Lawrence Berkeley National Laboratory.
Funding Information:
This work was supported by a grant from Shriners Hospital for Children.
PY - 2009/9/25
Y1 - 2009/9/25
N2 - 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.
AB - 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.
KW - collagens XVIII and XV
KW - crystal structure
KW - endostatin
KW - non-collagenous domain
KW - trimerization domain
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U2 - 10.1016/j.jmb.2009.07.057
DO - 10.1016/j.jmb.2009.07.057
M3 - Article
C2 - 19631658
AN - SCOPUS:69549130585
SN - 0022-2836
VL - 392
SP - 787
EP - 802
JO - Journal of molecular biology
JF - Journal of molecular biology
IS - 3
ER -