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.


2d03

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2d03.gif|left|200px]]<br /><applet load="2d03" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2d03.gif|left|200px]]
-
caption="2d03, resolution 1.97&Aring;" />
+
 
-
'''Crystal structure of the G91S mutant of the NNA7 Fab'''<br />
+
{{Structure
 +
|PDB= 2d03 |SIZE=350|CAPTION= <scene name='initialview01'>2d03</scene>, resolution 1.97&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of the G91S mutant of the NNA7 Fab'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2D03 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MES:'>MES</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D03 OCA].
+
2D03 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D03 OCA].
==Reference==
==Reference==
-
Crystallographic analysis of the NNA7 Fab and proposal for the mode of human blood-group recognition., Xie K, Song SC, Spitalnik SL, Wedekind JE, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1386-94. Epub 2005, Sep 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16204891 16204891]
+
Crystallographic analysis of the NNA7 Fab and proposal for the mode of human blood-group recognition., Xie K, Song SC, Spitalnik SL, Wedekind JE, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1386-94. Epub 2005, Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16204891 16204891]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 22: Line 31:
[[Category: antibody]]
[[Category: antibody]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:03 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:21:41 2008''

Revision as of 14:21, 20 March 2008


PDB ID 2d03

Drag the structure with the mouse to rotate
, resolution 1.97Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the G91S mutant of the NNA7 Fab


Overview

The NNA7 Fab antibody fragment recognizes the human N-type blood-group antigen comprised of the N-terminal glycopeptide of glycophorin A (GPA). A mutant form of this Fab fragment, NNA7-G91S, exhibits markedly reduced antigen binding. To provide insight into how these Fab fragments recognize this glycopeptide antigen, the crystal structures of NNA7 and NNA7-G91S were solved and refined to 1.83 and 1.97 A resolution, respectively. Both molecules are composed of the same heavy (H) chain Fd fragment, but each contains a slightly different light (L) chain owing to the G91S substitution. Specifically, the G91S mutation pushes the backbone of the neighboring H chain away from complementarity-determining region 3 (CDR3) of the L-chain variable region, allowing an additional glycerol cryoprotectant molecule to enter the antigen-combining site near the putative location of O-linked glycosylation. Each Fab fragment also possesses a well defined 2-(N-morpholino)ethanesulfonic acid (MES) molecule trapped in its antigen-combining site, as well as a crystallographic symmetry-related molecule comprising an amino-acid sequence that is virtually identical to the N-terminus of GPA. The MES molecule interacts with the H-chain CDR in a manner reminiscent of antibody-carbohydrate complexes. These results suggest a model for recognition of the glycopeptide antigen that accounts for the deleterious effect of the G91S substitution.

About this Structure

2D03 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of the NNA7 Fab and proposal for the mode of human blood-group recognition., Xie K, Song SC, Spitalnik SL, Wedekind JE, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1386-94. Epub 2005, Sep 28. PMID:16204891

Page seeded by OCA on Thu Mar 20 16:21:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools