1dl7: Difference between revisions

Revision as of 23:14, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1dl7.png

Template:STRUCTURE 1dl7

THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINETHE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE

Template:ABSTRACT PUBMED 10859335

About this StructureAbout this Structure

Full crystallographic information is available from OCA.

ReferenceReference

The structural basis of repertoire shift in an immune response to phosphocholine., Brown M, Schumacher MA, Wiens GD, Brennan RG, Rittenberg MB, J Exp Med. 2000 Jun 19;191(12):2101-12. PMID:10859335

Page seeded by OCA on Mon Jun 30 23:14:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1dl7.gif|left|200px]]
+{{Seed}}
+[[Image:1dl7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dl7|  PDB=1dl7  |  SCENE=  }}
-'''THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE'''
+===THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO PHOSPHOCHOLINE===
-==Overview==
+<!--
-The immune response to phosphocholine (PC)-protein is characterized by a shift in antibody repertoire as the response progresses. This change in expressed gene combinations is accompanied by a shift in fine specificity toward the carrier, resulting in high affinity to PC-protein. The somatically mutated memory hybridoma, M3C65, possesses high affinity for PC-protein and the phenyl-hapten analogue, p-nitrophenyl phosphocholine (NPPC). Affinity measurements using related PC-phenyl analogues, including peptides of varying lengths, demonstrate that carrier determinants contribute to binding affinity and that somatic mutations alter this recognition. The crystal structure of an M3C65-NPPC complex at 2.35-A resolution allows evaluation of the three light chain mutations that confer high-affinity binding to NPPC. Only one of the mutations involves a contact residue, whereas the other two have indirect effects on the shape of the combining site. Comparison of the M3C65 structure to that of T15, an antibody dominating the primary response, provides clear structural evidence for the role of carrier determinants in promoting repertoire shift. These two antibodies express unrelated variable region heavy and light chain genes and represent a classic example of the effect of repertoire shift on maturation of the immune response.
+The line below this paragraph, {{ABSTRACT_PUBMED_10859335}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10859335 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10859335}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Repertoire shift]]
 [[Category: Single chain fv]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:58:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:14:23 2008''