1fat: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fat OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fat RCSB], [http://www.ebi.ac.uk/pdbsum/1fat PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fat OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fat RCSB], [http://www.ebi.ac.uk/pdbsum/1fat PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/PHAL_PHAVU PHAL_PHAVU]] This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 18:28, 25 December 2014
PHYTOHEMAGGLUTININ-LPHYTOHEMAGGLUTININ-L
Structural highlights
Function[PHAL_PHAVU] This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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