2bx5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2bx5.jpg|left|200px]]
[[Image:2bx5.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2bx5 |SIZE=350|CAPTION= <scene name='initialview01'>2bx5</scene>, resolution 2.7&Aring;
+
The line below this paragraph, containing "STRUCTURE_2bx5", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2bx5| PDB=2bx5 | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bx5 OCA], [http://www.ebi.ac.uk/pdbsum/2bx5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bx5 RCSB]</span>
+
-
}}
+
'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL'''
'''IS FR1 THE ANTIBODY'S ACHILLIES HEEL'''
Line 26: Line 23:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: James, L C.]]
[[Category: James, L C.]]
-
[[Category: aggregation]]
+
[[Category: Aggregation]]
-
[[Category: amyloid]]
+
[[Category: Amyloid]]
-
[[Category: antibody]]
+
[[Category: Antibody]]
-
[[Category: fr1]]
+
[[Category: Fr1]]
-
[[Category: lcdd]]
+
[[Category: Lcdd]]
-
[[Category: light-chain]]
+
[[Category: Light-chain]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:55:19 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:13:07 2008''
+

Revision as of 17:55, 3 May 2008

Template:STRUCTURE 2bx5

IS FR1 THE ANTIBODY'S ACHILLIES HEEL


Overview

Antibodies are the archetypal molecules of the Ig-fold superfamily. Their highly conserved beta-sheet architecture has evolved to avoid aggregation by protecting edge strands. However, the crystal structure of a human V kappa domain described here, reveals an exposed beta-edge strand which mediates assembly of a helical pentadecameric oligomer. This edge strand is highly conserved in V kappa domains but is both shortened and capped by the use of two sequential trans-proline residues in V lambda domains. We suggest that the exposure of this beta-edge in V kappa domains may explain why light-chain deposition disease is mediated predominantly by kappa antibodies.

About this Structure

2BX5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Beta-edge interactions in a pentadecameric human antibody V kappa domain., James LC, Jones PC, McCoy A, Tennent GA, Pepys MB, Famm K, Winter G, J Mol Biol. 2007 Mar 30;367(3):603-8. Epub 2006 Nov 3. PMID:17292396 Page seeded by OCA on Sat May 3 20:55:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools