Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes revealed by high-resolution X-ray crystallography

Han, Gye Won; Lee, Jae Young; Song, Hyun Kyu; Chang, Changsoo; Min, Kyung Soo; Moon, Jinho; Shin, Dongkun; Kopka, Mary L.; Sawaya, M.R.; Yuan, Hanna S.; Kim, Thomas D.; Choe, Juhui; Lim, Dori; Moon, Hee Jung; Suh, Se Won

doi:10.1006/jmbi.2001.4559

Cited by 166 publications

(191 citation statements)

References 40 publications

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“…However, the exact nature of the physiological ligands bound to group II CD1 molecules during inflammation to promote NKT cell activity is still elusive. The finding that PC molecules differing in acyl chain composition can bind to the recombinant protein confirms that mCD1d molecules display a relatively broad specificity for hydrocarbon chain length, similarly to fatty acid-binding proteins and nonspecific lipid-binding proteins (46,47). The absolute predominance of van der Waals' contacts together with the paucity of hydrogen bonding partners within the binding cavities impose a restraint only on the length of the ligand acyl chain.…”

Section: Discussionmentioning

confidence: 69%

Crystal Structure of Mouse CD1d Bound to the Self Ligand Phosphatidylcholine: A Molecular Basis for NKT Cell Activation

Giabbai¹,

Sidobre²,

Crispin

et al. 2005

The Journal of Immunology

116

108

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NKT cells are immunoregulatory lymphocytes whose activation is triggered by the recognition of lipid Ags in the context of the CD1d molecules by the TCR. In this study we present the crystal structure to 2.8 Å of mouse CD1d bound to phosphatidylcholine. The interactions between the ligand acyl chains and the CD1d molecule define the structural and chemical requirements for the binding of lipid Ags to CD1d. The orientation of the polar headgroup toward the C terminus of the α1 helix provides a rationale for the structural basis for the observed Vα chain bias in invariant NKT cells. The contribution of the ligand to the protein surface suggests a likely mode of recognition of lipid Ags by the NKT cell TCR.

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Section: Discussionmentioning

confidence: 69%

Crystal Structure of Mouse CD1d Bound to the Self Ligand Phosphatidylcholine: A Molecular Basis for NKT Cell Activation

Giabbai¹,

Sidobre²,

Crispin

et al. 2005

The Journal of Immunology

116

108

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“…Other than the conservation of this motif, the percentage of sequence identity of LTPG and structurally characterized LTPs is quite low. When the 75 amino acids comprising the LTP-like domain of LTPG are compared with the sequence of LTP from a maize (Zea mays) seedling (PDB 1MZL), which is the closest solved x-ray crystal structure (Han et al, 2001), identity is ;20%. Therefore, the predicted protein structure of LTPG was modeled.…”

Section: Ltpg Displays Lipid Binding Activitymentioning

confidence: 99%

Arabidopsis LTPG Is a Glycosylphosphatidylinositol-Anchored Lipid Transfer Protein Required for Export of Lipids to the Plant Surface

et al. 2009

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Plant epidermal cells dedicate more than half of their lipid metabolism to the synthesis of cuticular lipids, which seal and protect the plant shoot. The cuticle is made up of a cutin polymer and waxes, diverse hydrophobic compounds including very-long-chain fatty acids and their derivatives. How such hydrophobic compounds are exported to the cuticle, especially through the hydrophilic plant cell wall, is not known. By performing a reverse genetic screen, we have identified LTPG, a glycosylphosphatidylinositol-anchored lipid transfer protein that is highly expressed in the epidermis during cuticle biosynthesis in Arabidopsis thaliana inflorescence stems. Mutant plant lines with decreased LTPG expression had reduced wax load on the stem surface, showing that LTPG is involved either directly or indirectly in cuticular lipid deposition. In vitro 2-p-toluidinonaphthalene-6-sulfonate assays showed that recombinant LTPG has the capacity to bind to this lipid probe. LTPG was primarily localized to the plasma membrane on all faces of stem epidermal cells in the growing regions of inflorescence stems where wax is actively secreted. These data suggest that LTPG may function as a component of the cuticular lipid export machinery.

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“…In order to further analyze the subsequent sites and to judge whether the conserved structural features of LTP occurred, the whole sequence still used to be the sequence alignment in Figure 3, the results found that the sequences behind the mutating bases had no any changed in encoding amino acids, so we preliminary judged that the mutagenesis on the site might have occurred, resulting in translation termination, and further speculated that LaSCA2 might be a pseudo-gene occurred during the evolution process of SCA. For maize LTP, the 46 th of (Han et al, 2001), indicating that the two sites had highly conservative in the sequence. 1.4 Phylogenetic tree construction and secondary structure prediction of SCA Ten amino acid sequence of Lily SCA except LaSCA2 and fifty seven known amino acid sequences of other plant LTP were employed to do alignment analysis to build the phylogenetic tree ( Figure 4).…”

Section: Results and Analysismentioning

confidence: 99%

Cloning of SCA Gene Related to Pollen Tube Adhesion and Oriented Growth and Analysis of Gene Diversity in <i>Lilium spp.</i>

Wu¹,

Cui²,

Zhang³

et al. 2012

mpb

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Stigma/style cysteine-rich adhesin genes (SCA) were cloned from 'Tresor' (Lilium Asiatic Hybrids), 'White heaven' (Lilium Longiflorum Hybrids) and 'Caruso' (Lilium Oriental Hybrids) leaves by PCR approaches. In this research we obtained four gene copies in both of 'Tresor' and 'Caruse' genomes and three gene copies in 'White heaven' genome. The identities of the cloned SCA among the copies were in the ranges from 72.97% to 99.68%. There are two exons and one intron in all of cloned SCA sequence, which could be deduced immature protein with 113 or 115 amino acid residues (encoding mature protein with 91 amino acid residues) SCA protein contains an N-terminal signal peptide of typical LTP protein, eight conserved cysteine residues and two consensus pentapeptide motifs. The identities among the amino acid sequences were in range from 87.91% to 98.90% higher than that of the similarities of gene sequences. Alignment analysis of amino acid sequences of cloned SCAs showed there were some distinct differences of amino acid site existing in the tested three species of lily hybrids. The phylogenetic tree revealed the relationship of the cloned 11 amino acid sequences of SCA were all more close to LTP family of monocotyledons than that of dicotyledons, which were consistent with the conclusions of kinship in plant taxonomy.

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Structural basis of non-specific lipid binding in maize lipid-transfer protein complexes revealed by high-resolution X-ray crystallography

Cited by 166 publications

References 40 publications

Crystal Structure of Mouse CD1d Bound to the Self Ligand Phosphatidylcholine: A Molecular Basis for NKT Cell Activation

Crystal Structure of Mouse CD1d Bound to the Self Ligand Phosphatidylcholine: A Molecular Basis for NKT Cell Activation

Arabidopsis LTPG Is a Glycosylphosphatidylinositol-Anchored Lipid Transfer Protein Required for Export of Lipids to the Plant Surface

Cloning of SCA Gene Related to Pollen Tube Adhesion and Oriented Growth and Analysis of Gene Diversity in <i>Lilium spp.</i>

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