Model of β-Sheet of Muscle Fatty Acid Binding Protein of Locusta migratoria Displays Characteristic Topology.
The β-sheet of muscle fatty acid binding protein of Locusta migratoria (Lm-FABP) was modeled by employing 2-D NMR data and the Rigid Body Assembly method. The model shows the β-sheet to comprise ten β-strands arranged anti-parallel to each other. There is a β-bulge between Ser 13 and Gln 14 which is a difference from the published structure of β-sheet of bovine heart Fatty Acid Binding Protein. Also, a hydrophobic patch consisting of Ile 45, Phe 51, Phe 64 and Phe 66 is present on the surface which is characteristic of most Fatty Acid Binding Proteins. A "gap" is present between βD and βE that provides evidence for the presence of a portal or opening between the polypeptide chains which allows ligand fatty acids to enter the protein cavity and bind to the protein.
Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar-91431, Saudi Arabia.
Nadeem A
NA
Kizilbash
Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar-91431, Saudi Arabia.
Abdul
A
Hai
Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar-91431, Saudi Arabia.
Jamal
J
Alruwaili
Locusta migratoria; Muscle Fatty Acid Binding Protein; Nuclear Overhauser Effect; Portal hypothesis; β-sheet of Lm-FABP