7JRH

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

Summary for 7JRH

• Entry DOI: 10.2210/pdb7jrh/pdb
• Descriptor: Cyclic peptide ASP-GLN-TRP-MLE-GLN-VAL-ASP-ORD-GLU-VAL-THR-GLY-ILE-ILE-THR-ORD, CALCIUM ION (3 entities in total)
• Functional Keywords: medin, cyclic, hairpin, mof, framework, de novo protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 1939.24

Authors

Wierzbicki, M.,Howitz, W.J.,Nowick, J.S. (deposition date: 2020-08-12, release date: 2020-09-09, Last modification date: 2025-04-02)

Primary citation

Howitz, W.J.,Wierzbicki, M.,Cabanela, R.W.,Saliba, C.,Motavalli, A.,Tran, N.,Nowick, J.S.
Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from Medin 19-36 .
J.Am.Chem.Soc., 142:15870-15875, 2020

PubMed Abstract: Amyloidogenic peptides and proteins are rich sources of supramolecular assemblies. Sequences derived from well-known amyloids, including Aβ, 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 β-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 β-hairpin structures can serve as ligands and assemble with metal ions to form MOFs.

PubMed: 32816461
DOI: 10.1021/jacs.0c06143

Experimental method

X-RAY DIFFRACTION (1.32 Å)