Abstract:
:Lipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Buhot N,Douliez JP,Jacquemard A,Marion D,Tran V,Maume BF,Milat ML,Ponchet M,Mikès V,Kader JC,Blein JPdoi
10.1016/s0014-5793(01)03116-7keywords:
subject
Has Abstractpub_date
2001-11-30 00:00:00pages
27-30issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(01)03116-7journal_volume
509pub_type
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