Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes revealed by high-resolution X-ray crystallography1 1Edited by D. Rees

2001 ◽  
Vol 308 (2) ◽  
pp. 263-278 ◽  
Author(s):  
Gye Won Han ◽  
Jae Young Lee ◽  
Hyun Kyu Song ◽  
Changsoo Chang ◽  
Kyeongsik Min ◽  
...  
Keyword(s):  
High Resolution ◽  
Lipid Transfer Protein ◽  
Protein Complexes ◽  
Lipid Binding ◽  
Structural Basis ◽  
Lipid Transfer ◽  
X Ray ◽  
Transfer Protein ◽  
Specific Lipid

scholarly journals High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings

Structure ◽  
1995 ◽  
Vol 3 (2) ◽  
pp. 189-199 ◽  
Author(s):  
Dong Hae Shin ◽  
Jae Young Lee ◽  
Kwang Yeon Hwang ◽  
Kyeong Kyu Kim ◽  
Se Won Suh
Keyword(s):  
Crystal Structure ◽  
High Resolution ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Maize Seedlings ◽  
Transfer Protein ◽  
Specific Lipid

scholarly journals High-affinity binding of very-long-chain fatty acyl-CoA esters to the peroxisomal non-specific lipid-transfer protein (sterol carrier protein-2)

1999 ◽  
Vol 339 (1) ◽  
pp. 193-199 ◽  
Author(s):  
Tobias B. DANSEN ◽  
Jan WESTERMAN ◽  
Fred S. WOUTERS ◽  
Ronald J. A. WANDERS ◽  
Arie van HOEK ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Lipid Transfer Protein ◽  
Fatty Acyl ◽  
Lipid Binding ◽  
Tryptophan Residue ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid ◽  
Long Chain ◽  
Lipid Binding Site

Binding of fluorescent fatty acids to bovine liver non-specific lipid-transfer protein (nsL-TP) was assessed by measuring fluorescence resonance energy transfer (FRET) between the single tryptophan residue of nsL-TP and the fluorophore. Upon addition of pyrene dodecanoic acid (Pyr-C12) and cis-parinaric acid to nsL-TP, FRET was observed indicating that these fatty acids were accommodated in the lipid binding site closely positioned to the tryptophan residue. Substantial binding was observed only when these fatty acids were presented in the monomeric form complexed to β-cyclodextrin. As shown by time-resolved fluorescence measurements, translocation of Pyr-C12 from the Pyr-C12–β-cyclodextrin complex to nsL-TP changed dramatically the direct molecular environment of the pyrene moiety: i.e. the fluorescence lifetime of the directly excited pyrene increased at least by 25% and a distinct rotational correlation time of 7 ns was observed. In order to evaluate the affinity of nsL-TP for intermediates of the β-oxidation pathway, a binding assay was developed based on the ability of fatty acyl derivatives to displace Pyr-C12 from the lipid binding site as reflected by the reduction of FRET. Hexadecanoyl-CoA and 2-hexadecenoyl-CoA were found to bind readily to nsL-TP, whereas 3-hydroxyhexadecanoyl-CoA and 3-ketohexadecanoyl-CoA bound poorly. The highest affinities were observed for the very-long-chain fatty acyl-CoA esters (24:0-CoA, 26:0-CoA) and their enoyl derivatives (24:1-CoA, 26:1-CoA). Binding of non-esterified hexadecanoic acid and tetracosanoic acid (24:0) was negligible.

Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding

2005 ◽  
Vol 61 (4) ◽  
pp. 397-406 ◽  
Author(s):  
François Hoh ◽  
Jean-Luc Pons ◽  
Marie-Françoise Gautier ◽  
Frédéric de Lamotte ◽  
Christian Dumas
Keyword(s):  
Molecular Basis ◽  
Lipid Transfer Protein ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid

scholarly journals Impact of lipid binding on the tertiary structure and allergenic potential of Jug r 3, the non-specific lipid transfer protein from walnut

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Pawel Dubiela ◽  
Rebecca Del Conte ◽  
Francesca Cantini ◽  
Tomasz Borowski ◽  
Roberta Aina ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Lipid Transfer Protein ◽  
Lipid Binding ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Allergenic Potential ◽  
Specific Lipid

scholarly journals Structural Characterization of Act c 10.0101 and Pun g 1.0101—Allergens from the Non-Specific Lipid Transfer Protein Family

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 256
Author(s):  
Andrea O’Malley ◽  
Swanandi Pote ◽  
Ivana Giangrieco ◽  
Lisa Tuppo ◽  
Anna Gawlicka-Chruszcz ◽  
...  
Keyword(s):  
Immunoglobulin E ◽  
Lipid Transfer Protein ◽  
Mass Spectrometry Analysis ◽  
Lipid Transfer ◽  
Helical Structures ◽  
Spectrometry Analysis ◽  
X Ray Crystallography ◽  
Transfer Protein ◽  
Specific Lipid

(1) Background: Non-specific lipid transfer proteins (nsLTPs), which belong to the prolamin superfamily, are potent allergens. While the biological role of LTPs is still not well understood, it is known that these proteins bind lipids. Allergen nsLTPs are characterized by significant stability and resistance to digestion. (2) Methods: nsLTPs from gold kiwifruit (Act c 10.0101) and pomegranate (Pun g 1.0101) were isolated from their natural sources and structurally characterized using X-ray crystallography (3) Results: Both proteins crystallized and their crystal structures were determined. The proteins have a very similar overall fold with characteristic compact, mainly α-helical structures. The C-terminal sequence of Act c 10.0101 was updated based on our structural and mass spectrometry analysis. Information on proteins’ sequences and structures was used to estimate the risk of cross-reactive reactions between Act c 10.0101 or Pun g 1.0101 and other allergens from this family of proteins. (4) Conclusions: Structural studies indicate a conformational flexibility of allergens from the nsLTP family and suggest that immunoglobulin E binding to some surface regions of these allergens may depend on ligand binding. Both Act c 10.0101 and Pun g 1.0101 are likely to be involved in cross-reactive reactions involving other proteins from the nsLTP family.

Non-specific Lipid Transfer Protein (Can s 3) Is a Relevant Cannabis Allergen in North America

2021 ◽  
Vol 147 (2) ◽  
pp. AB171
Author(s):  
Henry Morelli ◽  
Cathy Thorpe ◽  
Ine Decuyper ◽  
Cali Loblundo ◽  
Khaldon Abbas ◽  
...  
Keyword(s):  
North America ◽  
Lipid Transfer Protein ◽  
Lipid Transfer ◽  
Transfer Protein ◽  
Specific Lipid
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