1kc5: Difference between revisions
New page: left|200px<br /> <applet load="1kc5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kc5, resolution 2.50Å" /> '''CRYSTAL STRUCTURE O... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1kc5.gif|left|200px]]<br /> | [[Image:1kc5.gif|left|200px]]<br /><applet load="1kc5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1kc5" size=" | |||
caption="1kc5, resolution 2.50Å" /> | caption="1kc5, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDE'''<br /> | '''CRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
Crystal structures of distinct mAbs that recognize a common epitope of a | Crystal structures of distinct mAbs that recognize a common epitope of a peptide Ag have been determined and analyzed in the unbound and bound forms. These Abs display dissimilar binding site structures in the absence of the Ag. The dissimilarity is primarily expressed in the conformations of complementarity-determining region H3, which is responsible for defining the epitope specificity. Interestingly, however, the three Abs exhibit similar complementarity-determining region conformations in the Ag binding site while recognizing the common epitope, indicating that different pathways of binding are used for Ag recognition. The epitope also exhibits conformational similarity when bound to each of these Abs, although the peptide Ag was otherwise flexible. The observed conformational convergence in the epitope and the Ag binding site was facilitated by the plasticity in the nature of interactions. | ||
==About this Structure== | ==About this Structure== | ||
1KC5 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:// | 1KC5 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=1KC5 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Nair, D | [[Category: Nair, D T.]] | ||
[[Category: Nayak, B | [[Category: Nayak, B P.]] | ||
[[Category: Rao, K | [[Category: Rao, K V.]] | ||
[[Category: Salunke, D | [[Category: Salunke, D M.]] | ||
[[Category: Siddiqui, Z.]] | [[Category: Siddiqui, Z.]] | ||
[[Category: Singh, K.]] | [[Category: Singh, K.]] | ||
| Line 24: | Line 23: | ||
[[Category: peptide antigen]] | [[Category: peptide antigen]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:24 2008'' | ||
Revision as of 14:32, 21 February 2008
|
CRYSTAL STRUCTURE OF ANTIBODY PC287 IN COMPLEX WITH PS1 PEPTIDE
OverviewOverview
Crystal structures of distinct mAbs that recognize a common epitope of a peptide Ag have been determined and analyzed in the unbound and bound forms. These Abs display dissimilar binding site structures in the absence of the Ag. The dissimilarity is primarily expressed in the conformations of complementarity-determining region H3, which is responsible for defining the epitope specificity. Interestingly, however, the three Abs exhibit similar complementarity-determining region conformations in the Ag binding site while recognizing the common epitope, indicating that different pathways of binding are used for Ag recognition. The epitope also exhibits conformational similarity when bound to each of these Abs, although the peptide Ag was otherwise flexible. The observed conformational convergence in the epitope and the Ag binding site was facilitated by the plasticity in the nature of interactions.
About this StructureAbout this Structure
1KC5 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Epitope recognition by diverse antibodies suggests conformational convergence in an antibody response., Nair DT, Singh K, Siddiqui Z, Nayak BP, Rao KV, Salunke DM, J Immunol. 2002 Mar 1;168(5):2371-82. PMID:11859128
Page seeded by OCA on Thu Feb 21 13:32:24 2008