1fat
From Proteopedia
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'''PHYTOHEMAGGLUTININ-L''' | '''PHYTOHEMAGGLUTININ-L''' | ||
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[[Category: Hamelryck, T.]] | [[Category: Hamelryck, T.]] | ||
[[Category: Loris, R.]] | [[Category: Loris, R.]] | ||
- | [[Category: | + | [[Category: Glycoprotein]] |
- | [[Category: | + | [[Category: Lectin]] |
- | [[Category: | + | [[Category: Plant defense protein]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:06:48 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 13:06, 2 May 2008
PHYTOHEMAGGLUTININ-L
Overview
The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed lectin from Phaseolus vulgaris, has been solved with molecular replacement using the coordinates of lentil lectin as model, and refined at a resolution of 2.8 A. The final R-factor of the structure is 20.0%. The quaternary structure of the PHA-L tetramer differs from the structures of the concanavalin A and peanut lectin tetramers, but resembles the structure of the soybean agglutinin tetramer. PHA-L consists of two canonical legume lectin dimers that pack together through the formation of a close contact between two beta-strands. Of the two covalently bound oligosaccharides per monomer, only one GlcNAc residue per monomer is visible in the electron density. In this article we describe the structure of PHA-L, and we discuss the putative position of the high affinity adenine-binding site present in a number of legume lectins. A comparison with transthyretin, a protein that shows a remarkable resemblance to PHA-L, gives further ground to our proposal.
About this Structure
1FAT is a Single protein structure of sequence from Phaseolus vulgaris. Full crystallographic information is available from OCA.
Reference
The crystallographic structure of phytohemagglutinin-L., Hamelryck TW, Dao-Thi MH, Poortmans F, Chrispeels MJ, Wyns L, Loris R, J Biol Chem. 1996 Aug 23;271(34):20479-85. PMID:8702788 Page seeded by OCA on Fri May 2 16:06:48 2008