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.

1mnu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mnu.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1mnu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mnu| PDB=1mnu | SCENE= }}
{{STRUCTURE_1mnu| PDB=1mnu | SCENE= }}
-
'''UNLIGANDED BACTERICIDAL ANTIBODY AGAINST NEISSERIA MENINGITIDIS'''
+
===UNLIGANDED BACTERICIDAL ANTIBODY AGAINST NEISSERIA MENINGITIDIS===
-
==Overview==
+
<!--
-
MN12H2 is a bactericidal antibody directed against outer membrane protein PorA epitope P1.16 of Neisseria meningitidis. Binding of MN12H2 to PorA at the meningococcal surface activates the classical complement pathway resulting in bacterial lysis. We have determined the crystal structure of the unliganded MN12H2 Fab fragment in two different crystal forms and compared it with the structure of the Fab in complex with a P1.16-derived peptide. The unliganded Fabs have elbow bend angles of 155 degrees and 159 degrees, whereas the liganded Fab has a more closed elbow bend of 143 degrees. Substantial differences in quaternary and tertiary structure of the antigen binding site are observed between the unliganded and liganded MN12H2 Fab structures that can be attributed to peptide binding. The variable light and heavy chain interface of the liganded Fab is twisted by a 5 degrees rotation along an axis approximately perpendicular to the plane of the interface. Hypervariable loops H1, H2, and framework loop FR-H3 follow this rotation. The hypervariable loop H3 undergoes conformational changes but remains closely linked to hypervariable loop L1. In contrast with the binding site expansion seen in other Fab-peptide structures, the MN12H2 binding site is narrowed upon peptide binding due to the formation of a "false floor" mediated by arginine residue 101 of the light chain. These results indicate that PorA epitope P1.16 of N. meningitidis is recognized by the complement-activating antibody MN12H2 through induced fit, allowing the formation of a highly complementary immune complex.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9880525}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9880525 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9880525}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Murine immunoglobulin igg2a kappa]]
[[Category: Murine immunoglobulin igg2a kappa]]
[[Category: Unliganded]]
[[Category: Unliganded]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:28:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:30:03 2008''

Revision as of 21:30, 2 July 2008

Image:1mnu.png

Template:STRUCTURE 1mnu

UNLIGANDED BACTERICIDAL ANTIBODY AGAINST NEISSERIA MENINGITIDIS

Template:ABSTRACT PUBMED 9880525

About this Structure

1MNU is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Bactericidal antibody recognition of meningococcal PorA by induced fit. Comparison of liganded and unliganded Fab structures., van den Elsen J, Vandeputte-Rutten L, Kroon J, Gros P, J Biol Chem. 1999 Jan 15;274(3):1495-501. PMID:9880525

Page seeded by OCA on Thu Jul 3 00:30:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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