Islet Amyloid Polypeptide (IAPP or Amylin) fused to Maltose Binding Protein

Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process

Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein

MMBP, Maltodextrin-binding protein, Amylin, Diabetes-associated peptide, DAP, Insulinoma amyloid peptide

MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEI
TPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWP
LIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAA
TMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAAAKCNTATCATQRLANFLVHSSNNFGAILSS
TNVGSNTY

2.0 M Ammonium Sulfate, 0.1M Sodium Acetate pH 4.6, vapor diffusion, hanging drop, temperature 298K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY

native fold for amyloidogenic protein, Sugar transport, Transport, Amidation, Amyloid, Cleavage on pair of basic residues, Hormone, Secreted, SUGAR BINDING PROTEIN

KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT
PDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPL
IAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAAT
MENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQT