Rossmann fold
The Rossmann fold is a protein structural motif found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD, and NADP.[1] The structure is composed of up to seven mostly parallel beta strands. The first two strands are connected by an α- helix. The structures of segments between additional strands vary greatly and may include structures such as short helical segments and coils.[1]
The motif is named for Michael Rossmann, who first pointed out that this is a frequently occurring motif in nucleotide binding proteins, such as dehydrogenases.[2]
In 1989, Israel Hanukoglu from the Weizmann Institute of Science discovered that the consensus sequence for NADP binding site in some enzymes that utilize NADP differs from the NAD binding motif.[3] This discovery was used to re-engineer coenzyme specificities of enzymes.[4]
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