2n1e

MAX1 peptide fibril

spinqualitylabelsall models 2n1e Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2n1e is a 8 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DPR, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Most, if not all, peptide- and protein-based hydrogels formed by self-assembly can be characterized as kinetically trapped 3D networks of fibrils. The propensity of disease-associated amyloid-forming peptides and proteins to assemble into polymorphic fibrils suggests that cross-beta fibrils comprising hydrogels may also be polymorphic. We use solid-state NMR to determine the molecular and supramolecular structure of MAX1, a de novo designed gel-forming peptide, in its fibrillar state. We find that MAX1 adopts a beta-hairpin conformation and self-assembles with high fidelity into a double-layered cross-beta structure. Hairpins assemble with an in-register Syn orientation within each beta-sheet layer and with an Anti orientation between layers. Surprisingly, although the MAX1 fibril network is kinetically trapped, solid-state NMR data show that fibrils within this network are monomorphic and most likely represent the thermodynamic ground state. Intermolecular interactions not available in alternative structural arrangements apparently dictate this monomorphic behavior. Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network.,Nagy-Smith K, Moore E, Schneider J, Tycko R Proc Natl Acad Sci U S A. 2015 Jul 27. pii: 201509313. PMID:26216960 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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