Os03g0111300 - Revision history

Rice2012: /* Structured Information */

2015-06-12T04:57:49Z

‎Structured Information

Yilutongxing: /* Fatty acids binds affinity */

2014-06-08T14:57:50Z

‎Fatty acids binds affinity

Sancunriguang: /* Potential application in drug delivery */

2014-06-08T14:53:09Z

‎Potential application in drug delivery

Gylu: /* Reference */

2014-06-08T14:29:04Z

‎Reference

Gylu: /* Structure information */

2014-06-08T14:28:09Z

‎Structure information

Gylu: /* Structure information */

2014-06-08T14:26:19Z

‎Structure information

Gylu: /* Structure information */

2014-06-08T14:06:33Z

‎Structure information

Gylu: /* Reference */

2014-06-08T13:59:11Z

‎Reference

Gylu: /* Structure information= */

2014-06-08T13:58:04Z

‎Structure information=

Gylu: /* Structure information= */

2014-06-08T13:56:07Z

‎Structure information=

@@ Line 175: / Line 175: @@
 ==Structured Information==
 [[Category:Genes]]
 [[Category:Japonica mRNA]]

← Older revision		Revision as of 14:57, 8 June 2014
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	=='''Fatty acids binds affinity'''==		=='''Fatty acids binds affinity'''==
		+	Fatty acids binds affinity
		+	A computational study was carried out to identify the structural determinant controlling the affinity, specificity and binding strength of several saturated and unsaturated fatty acids with Oryza sativa(Indica group) nonspecific lipid transfer protein(nsLTP2).Association between the number, position and conformation of hydrophobic patches and lipid binding properties of the protein was evidenced by docking analysis .Binding affinity is influenced by the number of carbon atoms, location of double bonds and hydroxyl group in the acyl chain. The results may direct at developing application sinLTP-mediated transport and control led release o flow molecular weight drugs [8]
		+	The results would pave the routes for application of current methodology in nsLTP structural properties and may provide a convenient plat form for the development of protein-based drug carriers. The results would pave the routes for application of current methodology in nsLTP structural properties and may provide a convenient plat form for the development of protein-based drug carriers.
		+	Plant nonspecific lipid transfer protein 2 (nsLTP2)
		+	is a small (7 kDa) protein that binds lipid-like
		+	ligands. An inner hydrophobic cavity surrounded by
		+	a-helices is the defining structural feature of
		+	nsLTP2. Although nsLTP2 structures have been
		+	reported earlier, the detailed mechanisms of ligand
		+	binding and lipid transfer remain unclear. In this
		+	study, we used site-directed mutagenesis to determine
		+	the role of various hydrophobic residues (L8,
		+	I15, F36, F39, Y45, Y48, and V49) in the structure,
		+	stability, ligand binding, and lipid transfer activity
		+	of rice nsLTP2. Three single mutations (L8A, F36A,
		+	and V49A) drastically alter the native tertiary
		+	structure and perturb ligand binding and lipid
		+	transfer activity. Therefore, these three residues are
		+	structurally important. The Y45A mutant, however,
		+	retains a native-like structure but has decreased
		+	lipid binding affinity and lipid transfer activity,
		+	implying that this aromatic residue is critical for
		+	these biological functions. The mutants, I15A and
		+	Y48A, exhibit quite different ligand binding affinities.
		+	Y48 is involved in planar sterol binding but
		+	not linear lysophospholipid association. As for
		+	I15A, it had the highest dehydroergosterol binding
		+	affinity in spite of the lower lipid binding and
		+	transfer abilities. Our results suggest that the long
		+	alkyl side chain of I15 would restrict the flexibility
		+	of loop I (G13-A19) for sterol entry. Finally, F39A
		+	can markedly increase the exposed hydrophobic surface
		+	to maintain its transfer efficiency despite
		+	reduced ligand binding affinity. These findings suggest
		+	that the residues forming the hydrophobic cavity
		+	play various important roles in the structure
		+	and function of rice nsLTP2.

	=='''Reference'''==		=='''Reference'''==

← Older revision		Revision as of 14:53, 8 June 2014
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	=='''Potential application in drug delivery'''==		=='''Potential application in drug delivery'''==
		+	Potential application in drug delivery
		+	Plant non-specific lipid-transfer proteins (nsLTPs) have received an increasing interest as potential drug carriers in drug delivery systems.
		+	NsLTPs are subdivided into nsLTP1 (9 kDa) and nsLTP2 (7 kDa) according to the molecular weight. All of nsLTPs are highly stable proteins
		+	because they possess eight highly conserved cysteine residues forming four disulfide bonds. These highly stable proteins can protect drugs
		+	against oxidation or degradation. In this paper, the application of nsLTPs in a drug carrier systemwas comprehended through scanning chemical
		+	compounds to obtain the potential nsLTPs-binding drugs from the comprehensive medicinal chemistry (CMC) database. These results helped
		+	us to realize the binding differences for preferred drugs between maize nsLTP1 and rice nsLTP2. We have successfully constructed a rice
		+	nsLTP2 mutant (Y45W) to improve fluorescence sensitivity. The fluorescence binding assay showed that nsLTP2 can associate with sterol-like
		+	or triphenylmethane-like molecules but the binding affinities of nsLTP2 with both of nsLTP2-binding drug candidates are quite different.
		+	Dissociation constants (Kd) for sterol/nsLTP2 complexes is below one micromolar and it is sufficient for these molecules to slowly release in
		+	a controlled-release drug delivery process. In addition, titration curve shows that binding model for nsLTP2 with the triphenylmethyl moiety
		+	of the molecule is more complicated. The basic triphenyl ring system may be critical for the nsLTP2 association. These results imply that rice
		+	nsLTP2 have highly potential applications in pharmaceuticals. The procedure combined a unique computer-based high throughput screening
		+	(HTS) method with an experimental binding assay, can effectively determine potential nsLTPs-binding drugs from the compound library, thus
		+	increasing the added value of nsLTPs in a drug carrier system. [7]
		+
	=='''Fatty acids binds affinity'''==		=='''Fatty acids binds affinity'''==

@@ Line 116: / Line 116: @@
 [6]Solution Structure of Plant Nonspecific Lipid Transfer Protein-2
 from Rice (Oryza sativa)*(2012) Ping-Chiang Lyu
 ==Structured Information==

← Older revision		Revision as of 14:28, 8 June 2014
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	[[File:Figure 2]]		[[File:Figure 2]]
		+
		+	=='''Potential application in drug delivery'''==
		+	=='''Fatty acids binds affinity'''==

	=='''Reference'''==		=='''Reference'''==

@@ Line 16: / Line 16: @@
 =='''Structure information'''==
    The structure of nsLTP2 was obtained using
-distance constraints, 30 hydrogen bond constraints,
+The structure of nsLTP2 was obtained using 813 distance constraints, 30 hydrogen bond constraints,
 and 19 dihedral angle constraints. Fifteen of the 50 random
 simulated annealing structures satisfied all of the

@@ Line 15: / Line 15: @@
 Transfer lipids across membranes. May play a role in plant defense or in the biosynthesis of cuticle layers.
 =='''Structure information'''==
   The structure of nsLTP2 was obtained using
 distance constraints, 30 hydrogen bond constraints,
 and 19 dihedral angle constraints. Fifteen of the 50 random
@@ Line 33: / Line 34: @@
 plant defense proteins (As showed follow）[6]
+[[File:Figure 2]]
 =='''Reference'''==

@@ Line 59: / Line 59: @@
 [5]"Purification and characterization of a novel 7-kDa non-specific lipid transfer protein-2 from rice (Oryza sativa)."
 Liu Y.-J., Samuel D., Lin C.H., Lyu P.-C.
 ==Structured Information==

@@ Line 14: / Line 14: @@
 =='''Function'''==
 Transfer lipids across membranes. May play a role in plant defense or in the biosynthesis of cuticle layers.
-=='''Structure information'''===
+=='''Structure information'''==
   The structure of nsLTP2 was obtained using
 distance constraints, 30 hydrogen bond constraints,
@@ Line 31: / Line 31: @@
 sterols. The positively charged residues on the molecular
 surface of nsLTP2 are structurally similar to other
-plant defense proteins (As showed follow)
+plant defense proteins (As showed follow）[6]