1afh

<StructureSection load='1afh' size='340' side='right'caption='[[1afh]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1afh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afh OCA], [https://pdbe.org/1afh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1afh RCSB], [https://www.ebi.ac.uk/pdbsum/1afh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1afh ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/NLTP_MAIZE NLTP_MAIZE]] Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.

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== Publication Abstract from PubMed ==

The three-dimensional solution structure of a nonspecific lipid transfer protein extracted from maize seeds determined by 1H 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 (phi, psi, chi 1) derived from NOEs and 3J 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 alpha-class proteins. 1H NMR and fluorescence studies show that this protein forms well-defined complexes in aqueous solution with lysophosphatidylcholine. Dissociation constants, Kd, of 1.9 +/- 0.6 x 10(-6) M and &gt; 10(-3) M were obtained with lyso-C16 and -C12, respectively. A structure model for a lipid-protein complex is proposed in which the aliphatic chain of the phospholipid is inserted in the internal cavity and the polar head interacts with the charged side chains located at one end of this cavity. Our model for the lipid-protein complex is qualitatively very similar to the recently published crystal structure (Shin DH et al., 1995, Structure 3:189-199).

Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds.,Gomar J, Petit MC, Sodano P, Sy D, Marion D, Kader JC, Vovelle F, Ptak M Protein Sci. 1996 Apr;5(4):565-77. PMID:8845747<ref>PMID:8845747</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1afh" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Gomar, J]]

[[Category: Kader, J C]]

[[Category: Marion, D]]

[[Category: Petit, M C]]

[[Category: Ptak, M]]

[[Category: Sodano, P]]

[[Category: Sy, D]]

[[Category: Vovelle, F]]

[[Category: Molecular modeling]]