7jrh | pdb_00007jrh

X-ray crystal structure of a cyclic peptide containing medin(19-25) and medin(31-37)

spinqualitylabelsall models 7jrh, resolution 1.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.32Å Ligands: CA, MLE, ORN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Amyloidogenic peptides and proteins are rich sources of supramolecular assemblies. Sequences derived from well-known amyloids, including Abeta, human islet amyloid polypeptide, and tau have been found to assemble as fibrils, nanosheets, ribbons, and nanotubes. The supramolecular assembly of medin, a 50-amino acid peptide that forms fibrillary deposits in aging human vasculature, has not been heavily investigated. In this work, we present an X-ray crystallographic structure of a cyclic beta-sheet peptide derived from the 19-36 region of medin that assembles to form interpenetrating cubes. The edge of each cube is composed of a single peptide, and each vertex is occupied by a divalent metal ion. This structure may be considered a metal-organic framework (MOF) containing a large peptide ligand. This work demonstrates that peptides containing Glu or Asp that are preorganized to adopt beta-hairpin structures can serve as ligands and assemble with metal ions to form MOFs. Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from Medin19-36.,Howitz WJ, Wierzbicki M, Cabanela RW, Saliba C, Motavalli A, Tran N, Nowick JS J Am Chem Soc. 2020 Sep 3. doi: 10.1021/jacs.0c06143. PMID:32816461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA