1igi: Difference between revisions

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[[Image:1igi.~~gif~~|left|200px]]

[[Image:1igi.png|left|200px]]

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~~'''~~26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY~~'''~~

===26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY===

~~==Overview==~~

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~~We have determined the three~~-~~dimensional structures of the antigen~~-~~binding fragment of~~ the ~~anti-digoxin monoclonal antibody 26-10 in~~ the ~~uncomplexed state at 2.7 A resolution and~~ as ~~a complex with digoxin~~ at 2.~~5 A resolution~~. ~~Neither the antibody nor digoxin undergoes any significant conformational changes upon forming the complex. Digoxin interacts primarily with the antibody heavy chain and~~ is ~~oriented such that the carbohydrate groups are exposed to solvent and~~ the ~~lactone ring is buried in a deep pocket at the bottom of the combining site~~. ~~Despite extensive interactions between antibody and antigen, no hydrogen bonds or salt links are formed between 26~~-~~10 and digoxin. Thus the 26~~-~~10-digoxin complex is unique among the known three-dimensional structures of antibody-antigen complexes in that specificity and high affinity arise primarily from shape complementarity.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8234291}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8234291 is the PubMed ID number.

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==About this Structure==

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[[Category: Sheriff, S.]]

[[Category: Immunoglobulin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 19~~:58:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 11:01:26 2008''

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-[[Image:1igi.gif|left|200px]]
+{{Seed}}
+[[Image:1igi.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1igi|  PDB=1igi  |  SCENE=  }}
-'''26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY'''
+===26-10 FAB:DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY===
-==Overview==
+<!--
-We have determined the three-dimensional structures of the antigen-binding fragment of the anti-digoxin monoclonal antibody 26-10 in the uncomplexed state at 2.7 A resolution and as a complex with digoxin at 2.5 A resolution. Neither the antibody nor digoxin undergoes any significant conformational changes upon forming the complex. Digoxin interacts primarily with the antibody heavy chain and is oriented such that the carbohydrate groups are exposed to solvent and the lactone ring is buried in a deep pocket at the bottom of the combining site. Despite extensive interactions between antibody and antigen, no hydrogen bonds or salt links are formed between 26-10 and digoxin. Thus the 26-10-digoxin complex is unique among the known three-dimensional structures of antibody-antigen complexes in that specificity and high affinity arise primarily from shape complementarity.
+The line below this paragraph, {{ABSTRACT_PUBMED_8234291}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8234291 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8234291}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Sheriff, S.]]
 [[Category: Immunoglobulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:58:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 11:01:26 2008''