2f19

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="2f19" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f19, resolution 2.8&Aring;" /> '''THREE-DIMENSIONAL ST...)
Line 1: Line 1:
-
[[Image:2f19.gif|left|200px]]<br />
+
[[Image:2f19.gif|left|200px]]<br /><applet load="2f19" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="2f19" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="2f19, resolution 2.8&Aring;" />
caption="2f19, resolution 2.8&Aring;" />
'''THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY'''<br />
'''THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY'''<br />
==Overview==
==Overview==
-
The three-dimensional structure of FabR19.9 from a well-characterized, anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray, diffraction techniques in two crystalline forms (I and II) to a resolution, of 2.8 and 2.7 A, respectively. Essentially the same tertiary and, quaternary structure of the Fab is observed in the two forms. The major, difference resides in the intermolecular contacts, which are interpreted, to favor an irreversible transition from the metastable form I to the more, stable form II. The third complementarity-determining region of the heavy, chain (H3) folds back over the combining site and requires rearrangement, for hapten binding. This dynamic requirement on H3 is consistent with its, mobility in the structure and can explain hapten binding to an otherwise, inaccessible antibody combining site.
+
The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site.
==About this Structure==
==About this Structure==
-
2F19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure superseeds the now removed PDB entry 1F19. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F19 OCA].
+
2F19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure supersedes the now removed PDB entry 1F19. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F19 OCA].
==Reference==
==Reference==
Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody., Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A, Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1409652 1409652]
Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody., Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A, Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1409652 1409652]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Alzari, P.M.]]
+
[[Category: Alzari, P M.]]
-
[[Category: Lascombe, M.B.]]
+
[[Category: Lascombe, M B.]]
[[Category: Nisonoff, A.]]
[[Category: Nisonoff, A.]]
-
[[Category: Poljak, R.J.]]
+
[[Category: Poljak, R J.]]
[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:49:22 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:47 2008''

Revision as of 15:16, 21 February 2008


2f19, resolution 2.8Å

Drag the structure with the mouse to rotate

THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY

Overview

The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site.

About this Structure

2F19 is a Single protein structure of sequence from [1]. This structure supersedes the now removed PDB entry 1F19. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody., Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A, Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:1409652

Page seeded by OCA on Thu Feb 21 17:16:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools