1kcr
From Proteopedia
(New page: 200px<br /> <applet load="1kcr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kcr, resolution 2.90Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1kcr.gif|left|200px]]<br /> | + | [[Image:1kcr.gif|left|200px]]<br /><applet load="1kcr" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1kcr, resolution 2.90Å" /> | caption="1kcr, resolution 2.90Å" /> | ||
'''CRYSTAL STRUCTURE OF ANTIBODY PC283 IN COMPLEX WITH PS1 PEPTIDE'''<br /> | '''CRYSTAL STRUCTURE OF ANTIBODY PC283 IN COMPLEX WITH PS1 PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of Fab of an Ab PC283 complexed with its | + | The crystal structure of Fab of an Ab PC283 complexed with its corresponding peptide Ag, PS1 (HQLDPAFGANSTNPD), derived from the hepatitis B virus surface Ag was determined. The PS1 stretch Gln2P to Phe7P is present in the Ag binding site of the Ab, while the next three residues of the peptide are raised above the binding groove. The residues Ser11P, Thr12P, and Asn13P then loop back onto the Ag-binding site of the Ab. The last two residues, Pro14P and Asp15P, extend outside the binding site without forming any contacts with the Ab. The PC283-PS1 complex is among the few examples where the light chain complementarity-determining regions show more interactions than the heavy chain complementarity-determining regions, and a distal framework residue is involved in Ag binding. As seen from the crystal structure, most of the contacts between peptide and Ab are through the five residues, Leu3-Asp4-Pro5-Ala6-Phe7, of PS1. The paratope is predominantly hydrophobic with aromatic residues lining the binding pocket, although a salt bridge also contributes to stabilizing the Ag-Ab interaction. The molecular surface area buried upon PS1 binding is 756 A(2) for the peptide and 625 A(2) for the Fab, which is higher than what has been seen to date for Ab-peptide complexes. A comparison between PC283 structure and a homology model of its germline ancestor suggests that paratope optimization for PS1 occurs by improving both charge and shape complementarity. |
==About this Structure== | ==About this Structure== | ||
| - | 1KCR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1KCR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1KCR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Nair, D | + | [[Category: Nair, D T.]] |
| - | [[Category: Rao, K | + | [[Category: Rao, K V.S.]] |
[[Category: Sahu, N.]] | [[Category: Sahu, N.]] | ||
| - | [[Category: Salunke, D | + | [[Category: Salunke, D M.]] |
[[Category: Singh, K.]] | [[Category: Singh, K.]] | ||
[[Category: antibody]] | [[Category: antibody]] | ||
[[Category: peptide antigen complex (antibody/peptide)]] | [[Category: peptide antigen complex (antibody/peptide)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:35 2008'' |
Revision as of 11:32, 21 February 2008
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CRYSTAL STRUCTURE OF ANTIBODY PC283 IN COMPLEX WITH PS1 PEPTIDE
Overview
The crystal structure of Fab of an Ab PC283 complexed with its corresponding peptide Ag, PS1 (HQLDPAFGANSTNPD), derived from the hepatitis B virus surface Ag was determined. The PS1 stretch Gln2P to Phe7P is present in the Ag binding site of the Ab, while the next three residues of the peptide are raised above the binding groove. The residues Ser11P, Thr12P, and Asn13P then loop back onto the Ag-binding site of the Ab. The last two residues, Pro14P and Asp15P, extend outside the binding site without forming any contacts with the Ab. The PC283-PS1 complex is among the few examples where the light chain complementarity-determining regions show more interactions than the heavy chain complementarity-determining regions, and a distal framework residue is involved in Ag binding. As seen from the crystal structure, most of the contacts between peptide and Ab are through the five residues, Leu3-Asp4-Pro5-Ala6-Phe7, of PS1. The paratope is predominantly hydrophobic with aromatic residues lining the binding pocket, although a salt bridge also contributes to stabilizing the Ag-Ab interaction. The molecular surface area buried upon PS1 binding is 756 A(2) for the peptide and 625 A(2) for the Fab, which is higher than what has been seen to date for Ab-peptide complexes. A comparison between PC283 structure and a homology model of its germline ancestor suggests that paratope optimization for PS1 occurs by improving both charge and shape complementarity.
About this Structure
1KCR is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of an antibody bound to an immunodominant peptide epitope: novel features in peptide-antibody recognition., Nair DT, Singh K, Sahu N, Rao KV, Salunke DM, J Immunol. 2000 Dec 15;165(12):6949-55. PMID:11120821
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