3HSH
Crystal structure of human collagen XVIII trimerization domain (Tetragonal crystal form)
Summary for 3HSH
| Entry DOI | 10.2210/pdb3hsh/pdb |
| Related | 3HON |
| Descriptor | Collagen alpha-1(XVIII) chain, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | collagen, extracellular matrix, basement membrane, collagen xviii, trimerization domain, folding, association, chain selection, endostatin, triple helix, alternative promoter usage, cell adhesion, disulfide bond, glycoprotein, hydroxylation, metal-binding, secreted, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted, extracellular space, extracellular matrix : P39060 |
| Total number of polymer chains | 6 |
| Total formula weight | 40731.87 |
| Authors | Boudko, S.P.,Bachinger, H.P. (deposition date: 2009-06-10, release date: 2009-08-11, Last modification date: 2024-02-21) |
| Primary citation | Boudko, S.P.,Sasaki, T.,Engel, J.,Lerch, T.F.,Nix, J.,Chapman, M.S.,Bachinger, H.P. Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold. J.Mol.Biol., 392:787-802, 2009 Cited by PubMed Abstract: 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. PubMed: 19631658DOI: 10.1016/j.jmb.2009.07.057 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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