2d03: Difference between revisions

Revision as of 03:29, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2d03.png

Template:STRUCTURE 2d03

Crystal structure of the G91S mutant of the NNA7 FabCrystal structure of the G91S mutant of the NNA7 Fab

Template:ABSTRACT PUBMED 16204891

About this StructureAbout this Structure

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

ReferenceReference

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

Purification, crystallization and X-ray diffraction analysis of a recombinant Fab that recognizes a human blood-group antigen., Song SC, Xie K, Czerwinski M, Spitalnik SL, Wedekind JE, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):788-91. Epub 2004, Mar 23. PMID:15039587

Page seeded by OCA on Tue Jul 29 03:29:50 2008

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OCA

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-[[Image:2d03.gif|left|200px]]
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 {{STRUCTURE_2d03|  PDB=2d03  |  SCENE=  }}
-'''Crystal structure of the G91S mutant of the NNA7 Fab'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16204891}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16204891 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16204891}}
 ==About this Structure==
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 ==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://www.ncbi.nlm.nih.gov/pubmed/16204891 16204891]
+Purification, crystallization and X-ray diffraction analysis of a recombinant Fab that recognizes a human blood-group antigen., Song SC, Xie K, Czerwinski M, Spitalnik SL, Wedekind JE, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):788-91. Epub 2004, Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15039587 15039587]
 [[Category: Mus musculus]]
 [[Category: Single protein]]
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 [[Category: Xie, K.]]
 [[Category: Antibody]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:29:50 2008''