We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1dbj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dbj.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1dbj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dbj| PDB=1dbj | SCENE= }}
{{STRUCTURE_1dbj| PDB=1dbj | SCENE= }}
-
'''MOLECULAR BASIS OF CROSS-REACTIVITY AND THE LIMITS OF ANTIBODY-ANTIGEN COMPLEMENTARITY'''
+
===MOLECULAR BASIS OF CROSS-REACTIVITY AND THE LIMITS OF ANTIBODY-ANTIGEN COMPLEMENTARITY===
-
==Overview==
+
<!--
-
Two major unanswered questions concerning the specificity of antibodies are: how do structurally different antigens bind with high affinity to the same antibody, and what are the limits of the antibody combining site complementarity and flexibility that contribute to such crossreactivity? We report here a comparative analysis of the X-ray structures of five conformationally different steroids in complex with the Fab' fragment of an anti-progesterone antibody DB3 at 2.7 A. This antibody is unable to complement completely the shape of the hydrophobic antigen so that crossreactivity occurs with other ligands without major structural rearrangements of the binding site. Antigen specificity can be explained through conserved interactions of DB3 with the steroid D-ring, whereas some of the crossreactivity is realized through different binding orientations of the steroid skeleton that place the A-ring into alternative pockets on the antibody surface. The restricted gene usage of the VGAM3.8 family in the generation of anti-progesterone monoclonal antibodies may be explained by the specific interaction of VH hallmark residues with the steroid D-ring. This first detailed structure of steroid interactions with a protein could be applied to the understanding of general mechanisms of steroid recognition as well as in the design of specific binding sites for small hydrophobic ligands.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8413674}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8413674 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8413674}}
==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Wilson, I A.]]
[[Category: Wilson, I A.]]
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:39:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:46:57 2008''

Revision as of 19:46, 30 June 2008

Image:1dbj.png

Template:STRUCTURE 1dbj

MOLECULAR BASIS OF CROSS-REACTIVITY AND THE LIMITS OF ANTIBODY-ANTIGEN COMPLEMENTARITY

Template:ABSTRACT PUBMED 8413674

About this Structure

1DBJ is a Protein complex structure. Full crystallographic information is available from OCA.

Reference

Molecular basis of crossreactivity and the limits of antibody-antigen complementarity., Arevalo JH, Taussig MJ, Wilson IA, Nature. 1993 Oct 28;365(6449):859-63. PMID:8413674

Page seeded by OCA on Mon Jun 30 22:46:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dbj"
Personal tools