Abstract
A basic, ninety two amino acid residue polypeptide, called CM4-3, was purified from seeds of Prosopis juliflora and sequenced. Sequence homology searches indicated that this protein is related to the nonspecific lipid transfer protein family (ns-LTP). A 3D model of CM4-3 was built base on the molecular coordinates of a maize ns-LTP and the obtained model revealed the presence of a highly conserved pocket formed by three a-helices capable of accommodating one molecule ofpalrnitic acid inside the CM4-3 structure.
Protein & Peptide Letters
Title:Amino acid sequence and molecular modeling of a lipid transfer protein from the seeds of prosopis juliflora and its interaction with palmitic acid
Volume: 7 Issue: 1
Author(s): Andre N ewton Monte Negreiros, Artur Torres Cordeiro and Carlos Bloch Jr.*
Affiliation:
- Universidade de Brasilia, Instituto de Quimica, 70910-900 Brasilia - DF, Brazil
- Embrapa/Cenargen, PO Box 02372, Brasilia, DF, Brazil
Abstract: A basic, ninety two amino acid residue polypeptide, called CM4-3, was purified from seeds of Prosopis juliflora and sequenced. Sequence homology searches indicated that this protein is related to the nonspecific lipid transfer protein family (ns-LTP). A 3D model of CM4-3 was built base on the molecular coordinates of a maize ns-LTP and the obtained model revealed the presence of a highly conserved pocket formed by three a-helices capable of accommodating one molecule ofpalrnitic acid inside the CM4-3 structure.
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Cite this article as:
Negreiros ewton Monte Andre N, Cordeiro Torres Artur and Bloch Jr. Carlos*, Amino acid sequence and molecular modeling of a lipid transfer protein from the seeds of prosopis juliflora and its interaction with palmitic acid, Protein & Peptide Letters 2000; 7 (1) . https://dx.doi.org/10.2174/092986650701221205150204
DOI https://dx.doi.org/10.2174/092986650701221205150204 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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