This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1fbi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fbi.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1fbi.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fbi| PDB=1fbi | SCENE= }}
{{STRUCTURE_1fbi| PDB=1fbi | SCENE= }}
-
'''CRYSTAL STRUCTURE OF A CROSS-REACTION COMPLEX BETWEEN FAB F9.13.7 AND GUINEA-FOWL LYSOZYME'''
+
===CRYSTAL STRUCTURE OF A CROSS-REACTION COMPLEX BETWEEN FAB F9.13.7 AND GUINEA-FOWL LYSOZYME===
-
==Overview==
+
<!--
-
The crystal structure of the complex between the cross-reacting antigen Guinea fowl lysozyme and the Fab from monoclonal antibody F9.13.7, raised against hen egg lysozyme, has been determined by x-ray diffraction to 3-A resolution. The antibody interacts with exposed residues of an alpha-helix and surrounding loops adjacent to the lysozyme active site cleft. The epitope of lysozyme bound by antibody F9.13.7 overlaps almost completely with that bound by antibody HyHEL10; the same 12 residues of the antigen interact with the two antibodies. The antibodies, however, have different combining sites with no sequence homology at any of their complementarity-determining regions and show a dissimilar pattern of cross-reactivity with heterologous antigens. Side chain mobility of epitope residues contributes to confer steric and electrostatic complementarity to differently shaped combining sites, allowing functional mimicry to occur. The capacity of two antibodies that have different fine specificities to bind the same area of the antigen emphasizes the operational character of the definition of an antigenic determinant. This example demonstrates that degenerate binding of the same structural motif does not require the existence of sequence homology or other chemical similarities between the different binding sites.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7629116}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7629116 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7629116}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Alzari, P M.]]
[[Category: Alzari, P M.]]
[[Category: Lescar, J.]]
[[Category: Lescar, J.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:08:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:00:05 2008''

Revision as of 00:00, 1 July 2008

Image:1fbi.png

Template:STRUCTURE 1fbi

CRYSTAL STRUCTURE OF A CROSS-REACTION COMPLEX BETWEEN FAB F9.13.7 AND GUINEA-FOWL LYSOZYME

Template:ABSTRACT PUBMED 7629116

About this Structure

1FBI is a Protein complex structure of sequences from Mus musculus and Numida meleagris. Full crystallographic information is available from OCA.

Reference

Crystal structure of a cross-reaction complex between Fab F9.13.7 and guinea fowl lysozyme., Lescar J, Pellegrini M, Souchon H, Tello D, Poljak RJ, Peterson N, Greene M, Alzari PM, J Biol Chem. 1995 Jul 28;270(30):18067-76. PMID:7629116

Page seeded by OCA on Tue Jul 1 03:00:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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