1cr7
From Proteopedia
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'''PEANUT LECTIN-LACTOSE COMPLEX MONOCLINIC FORM''' | '''PEANUT LECTIN-LACTOSE COMPLEX MONOCLINIC FORM''' | ||
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[[Category: Surolia, A.]] | [[Category: Surolia, A.]] | ||
[[Category: Vijayan, M.]] | [[Category: Vijayan, M.]] | ||
| - | [[Category: | + | [[Category: Acidic ph]] |
| - | [[Category: | + | [[Category: Lactose]] |
| - | [[Category: | + | [[Category: Lectin]] |
| - | [[Category: | + | [[Category: Legume lectin]] |
| - | [[Category: | + | [[Category: Monoclinic form]] |
| - | [[Category: | + | [[Category: Open quaternary structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:02:04 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:02, 2 May 2008
PEANUT LECTIN-LACTOSE COMPLEX MONOCLINIC FORM
Overview
The crystal structures of a monoclinic and a triclinic form of the peanut lectin-lactose complex, grown at pH 4.6, have been determined. They contain two and one crystallographically independent tetramers, respectively. The unusual "open" quaternary structure of the lectin, observed in the orthorhombic complex grown in neutral pH, is retained at the acidic pH. The sugar molecule is bound to three of the eight subunits in the monoclinic crystals, whereas the combining sites in four are empty. The lectin-sugar interactions are almost the same at neutral and acidic pH. A comparison of the sugar-bound and free subunits indicates that the geometry of the combining site is relatively unaffected by ligand binding. The combining site of the eighth subunit in the monoclinic crystals is bound to a peptide stretch in a loop from a neighboring molecule. The same interaction exists in two subunits of the triclinic crystals, whereas density corresponding to sugar exists in the combining sites of the other two subunits. Solution studies show that oligopeptides with sequences corresponding to that in the loop bind to the lectin at acidic pH, but only with reduced affinity at neutral pH. The reverse is the case with the binding of lactose to the lectin. A comparison of the neutral and acidic pH crystal structures indicates that the molecular packing in the latter is directed to a substantial extent by the increased affinity of the peptide loop to the combining site at acidic pH.
About this Structure
1CR7 is a Single protein structure of sequence from Arachis hypogaea. Full crystallographic information is available from OCA.
Reference
Crystal structures of the peanut lectin-lactose complex at acidic pH: retention of unusual quaternary structure, empty and carbohydrate bound combining sites, molecular mimicry and crystal packing directed by interactions at the combining site., Ravishankar R, Thomas CJ, Suguna K, Surolia A, Vijayan M, Proteins. 2001 May 15;43(3):260-70. PMID:11288176 Page seeded by OCA on Fri May 2 13:02:04 2008
