From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1rit.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rit.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1rit| PDB=1rit | SCENE= }} | | {{STRUCTURE_1rit| PDB=1rit | SCENE= }} |
| | | | |
| - | '''Crystal structure of Peanut lectin in complex with meso-tetrasulphonatophenylporphyrin and lactose'''
| + | ===Crystal structure of Peanut lectin in complex with meso-tetrasulphonatophenylporphyrin and lactose=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The extraordinary recognition specificity of lectins for carbohydrate ligands appears to be violated as they also bind to porphyrins and other noncarbohydrate ligands. In this study, crystal structures of meso-tetrasulfonatophenylporphyrin (H(2)TPPS) bound to peanut agglutinin (PNA) in the presence and absence of lactose were determined. The binding of H(2)TPPS with PNA involved 11 molecules of H(2)TPPS in different supramolecular stacking arrangements associated with a tetramer of PNA in the crystals of the PNA-H(2)TPPS binary complex as well as the PNA-H(2)TPPS-lactose ternary complex. The ternary complex involved lactose binding only to two subunits of the PNA tetramer, which did not have porphyrin interacting in the vicinity of the carbohydrate-binding site. Comparison of the two structures highlighted the plasticity of the carbohydrate-binding site expressed in terms of the conformational change in lactose binding. The unusual quaternary structure of PNA, which results in exposed protein-protein interaction sites, might be responsible for the porphyrin binding. The association of porphyrin in diverse oligomeric stacking arrangements observed in the PNA-H(2)TPPS complex suggested the possibility of protein-porphyrin aggregation under abnormal physiological conditions. The structures described here provide a possible native conformation of the carbohydrate-binding site of PNA in the absence of the ligand, highlight mapping of the unsaturated binding surfaces of PNA using porphyrin interactions, indicate new leads toward possible application of this lectin in photodynamic therapy, and exhibit diverse modes of porphyrin-lectin interactions with implications to porphyria, a disease that results from abnormal accumulation of porphyrins. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15823017}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15823017 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15823017}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Swamy, M J.]] | | [[Category: Swamy, M J.]] |
| | [[Category: Sugar binding protein]] | | [[Category: Sugar binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:32:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:19:25 2008'' |
Revision as of 06:19, 28 July 2008
Template:STRUCTURE 1rit
Crystal structure of Peanut lectin in complex with meso-tetrasulphonatophenylporphyrin and lactose
Template:ABSTRACT PUBMED 15823017
About this Structure
1RIT is a Single protein structure of sequence from Arachis hypogaea. Full crystallographic information is available from OCA.
Reference
Crystal structures of the PNA-porphyrin complex in the presence and absence of lactose: mapping the conformational changes on lactose binding, interacting surfaces, and supramolecular aggregations., Goel M, Damai RS, Sethi DK, Kaur KJ, Maiya BG, Swamy MJ, Salunke DM, Biochemistry. 2005 Apr 19;44(15):5588-96. PMID:15823017
Page seeded by OCA on Mon Jul 28 09:19:25 2008
