From Proteopedia
			(Difference between revisions)
												
			proteopedia linkproteopedia link
			
			
			
			
			
			
				 | 
				 | 
			
		| Line 1: | 
Line 1: | 
| - | [[Image:2q3n.gif|left|200px]]  | + | {{Seed}}  | 
|   | + | [[Image:2q3n.png|left|200px]]  | 
|   |  |   |  | 
|   | <!--  |   | <!--  | 
| Line 9: | 
Line 10: | 
|   | {{STRUCTURE_2q3n|  PDB=2q3n  |  SCENE=  }}   |   | {{STRUCTURE_2q3n|  PDB=2q3n  |  SCENE=  }}   | 
|   |  |   |  | 
| - | '''Agglutinin from Abrus Precatorius (APA-I)'''
  | + | ===Agglutinin from Abrus Precatorius (APA-I)===  | 
|   |  |   |  | 
|   |  |   |  | 
| - | ==Overview==
  | + | <!--   | 
| - | Abrin and agglutinin-I from the seeds of Abrus precatorius are type II ribosome-inactivating proteins that inhibit protein synthesis in eukaryotic cells. The two toxins share a high degree of sequence similarity; however, agglutinin-I is weaker in its activity. We compared the kinetics of protein synthesis inhibition by abrin and agglutinin-I in two different cell lines and found that approximately 200-2000-fold higher concentration of agglutinin-I is needed for the same degree of inhibition. Like abrin, agglutinin-I also induced apoptosis in the cells by triggering the intrinsic mitochondrial pathway, although at higher concentrations as compared with abrin. The reason for the decreased toxicity of agglutinin-I became apparent on the analysis of the crystal structure of agglutinin-I obtained by us in comparison with that of the reported structure of abrin. The overall protein folding of agglutinin-I is similar to that of abrin-a with a single disulfide bond holding the toxic A subunit and the lectin-like B-subunit together, constituting a heterodimer. However, there are significant differences in the secondary structural elements, mostly in the A chain. The substitution of Asn-200 in abrin-a with Pro-199 in agglutinin-I seems to be a major cause for the decreased toxicity of agglutinin-I. This perhaps is not a consequence of any kink formation by a proline residue in the helical segment, as reported by others earlier, but due to fewer interactions that proline can possibly have with the bound substrate.
  | + | The line below this paragraph, {{ABSTRACT_PUBMED_16772301}}, adds the Publication Abstract to the page   | 
|   | + | (as it appears on PubMed at http://www.pubmed.gov), where 16772301 is the PubMed ID number.  | 
|   | + | -->  | 
|   | + | {{ABSTRACT_PUBMED_16772301}}  | 
|   |  |   |  | 
|   | ==About this Structure==  |   | ==About this Structure==  | 
| Line 31: | 
Line 35: | 
|   | [[Category: Immunotoxin]]  |   | [[Category: Immunotoxin]]  | 
|   | [[Category: Ribosome-inactivating protein]]  |   | [[Category: Ribosome-inactivating protein]]  | 
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 14:16:04 2008''  | + |    | 
|   | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:01:14 2008''  | 
Revision as of 11:01, 27 July 2008
Template:STRUCTURE 2q3n 
 Agglutinin from Abrus Precatorius (APA-I)
Template:ABSTRACT PUBMED 16772301
 About this Structure
2Q3N is a Protein complex structure of sequences from Abrus precatorius. This structure supersedes the now removed PDB entry 2amz. Full crystallographic information is available from OCA. 
 Reference
Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin., Bagaria A, Surendranath K, Ramagopal UA, Ramakumar S, Karande AA, J Biol Chem. 2006 Nov 10;281(45):34465-74. Epub 2006 Jun 13. PMID:16772301
Page seeded by OCA  on Sun Jul 27 14:01:14 2008