Islet Amyloid Polypeptide (IAPP) Fibril Model
based on SSTNVG and NNFGAIL Peptide Crystal Structures
Summary: IAPP chains (red and blue)
Each successive strand in the spine is translated
by 4.8 Angstroms and rotated by -3.5 degrees.
The pitch length is 500 Angstroms.
The average radius is 45 Angstroms.
Current view: SSTNVG segements form the core of the fibril. Click here to see location of SSTNVG.
The segment NNFGAIL is on the outside edge of the fibril, forming a U-turn.
Click here to see location of NNFGAIL.
1) Four parallel beta sheets compose the spine of the fiber. Click here to see the four sheets colored separately.
The distance between the pairs of sheets is approximately 8.0 Angstroms.
2) The steric zipper side chains are shown in green.
The sheets are held together by Van der Waals forces, and a tight steric fit that excludes water molecules.
3) The asymmetric unit of the fibril is composed of two iapp molecules, shown here.
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