1k6f

Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3Crystal Structure of the Collagen Triple Helix Model [(Pro-Pro-Gly)10]3

Structural highlights 1k6f is a 6 chain structure with sequence from Saimiriine gammaherpesvirus 2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q80BK4_SHV2 Publication Abstract from PubMed The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)(10)](3) is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 A, using synchrotron radiation. The final model, which was refined to an R(factor) of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)(10)](3) packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils. Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3).,Berisio R, Vitagliano L, Mazzarella L, Zagari A Protein Sci. 2002 Feb;11(2):262-70. PMID:11790836 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Collagen 3D structures

spinqualitylabelsall models 1k6f, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image