3T4F
Crystal Structure of a KGE Collagen Mimetic Peptide at 1.68 A
Summary for 3T4F
| Entry DOI | 10.2210/pdb3t4f/pdb |
| Related | 3u29 6vzx |
| Descriptor | collagen mimetic peptide (2 entities in total) |
| Functional Keywords | collagen mimetic peptide, triple helix, biosynthetic protein |
| Biological source | synthetic construct (artificial sequence) |
| Total number of polymer chains | 6 |
| Total formula weight | 13370.25 |
| Authors | Fallas, J.A.,Dong, J.,Miller, M.D.,Tao, Y.J.,Hartgerink, J.D. (deposition date: 2011-07-25, release date: 2011-12-28, Last modification date: 2023-09-13) |
| Primary citation | Fallas, J.A.,Dong, J.,Tao, Y.J.,Hartgerink, J.D. Structural insights into charge pair interactions in triple helical collagen-like proteins. J.Biol.Chem., 287:8039-8047, 2012 Cited by PubMed Abstract: The collagen triple helix is the most abundant protein fold in humans. Despite its deceptively simple structure, very little is understood about its folding and fibrillization energy landscape. In this work, using a combination of x-ray crystallography and nuclear magnetic resonance spectroscopy, we carry out a detailed study of stabilizing pair-wise interactions between the positively charged lysine and the negatively charged amino acids aspartate and glutamate. We find important differences in the side chain conformation of amino acids in the crystalline and solution state. Structures from x-ray crystallography may have similarities to the densely packed triple helices of collagen fibers whereas solution NMR structures reveal the simpler interactions of isolated triple helices. In solution, two distinct types of contacts are observed: axial and lateral. Such register-specific interactions are crucial for the understanding of the registration process of collagens and the overall stability of proteins in this family. However, in the crystalline state, there is a significant rearrangement of the side chain conformation allowing for packing interactions between adjacent helices, which suggests that charged amino acids may play a dual role in collagen stabilization and folding, first at the level of triple helical assembly and second during fibril formation. PubMed: 22179819DOI: 10.1074/jbc.M111.296574 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.68 Å) |
Structure validation
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