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Solution Structure and Lipid Binding of a Nonspecific Lipid Transfer Protein Extracted from Maize Seeds by Jérôme Gomar; Marie‐Christine Petit; Patrick Sodano; Denise Sy; Didier Marion; Jean‐Claude Kader; Françoise Vovelle; Marius Ptak is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract The three‐dimensional solution structure of a nonspecific lipid transfer protein extracted from maize seeds determined by ^1^H NMR spectroscopy is described. This cationic protein consists of 93 amino acid residues. Its structure was determined from 1, 091 NOE‐derived distance restraints, including 929 interresidue connectivities and 197 dihedral restraints (__φ, ψ, χ__~1~) derived from NOEs and ^3^J coupling constants. The global fold involving four helical fragments connected by three loops and a C‐terminal tail without regular secondary structures is stabilized by four disulfide bridges. The most striking feature of this structure is the existence of an internal hydrophobic cavity running through the whole molecule. The global fold of this protein, very similar to that of a previously described lipid transfer protein extracted from wheat seeds (Gincel E et al., 1994, __Eur J Biochem 226__:413–422) constitutes a new architecture for __α__‐class proteins. ^1^H NMR and fluorescence studies show that this protein forms well‐defined complexes in aqueous solution with lysophosphatidylcholine. Dissociation constants, __K~d~__, of 1.9 ± 0.6 × 10^−6^ M and >10^−3^ M were obta

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Author

Jérôme Gomar; Marie‐Christine Petit; Patrick Sodano; Denise Sy; Didier Marion; Jean‐Claude Kader; Françoise Vovelle; Marius Ptak

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)