2bx5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==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.
+
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==
==About this Structure==
Line 13: Line 13:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: James, L.C.]]
+
[[Category: James, L C.]]
[[Category: aggregation]]
[[Category: aggregation]]
[[Category: amyloid]]
[[Category: amyloid]]
Line 21: Line 21:
[[Category: light-chain]]
[[Category: light-chain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:17:34 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:32 2008''

Revision as of 14:42, 21 February 2008


2bx5, resolution 2.7Å

Drag the structure with the mouse to rotate

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 Thu Feb 21 16:42:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools