1kcs
From Proteopedia
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| - | [[Image:1kcs.jpg|left|200px]] | + | [[Image:1kcs.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF ANTIBODY PC282 IN COMPLEX WITH PS1 PEPTIDE''' | + | {{Structure |
| + | |PDB= 1kcs |SIZE=350|CAPTION= <scene name='initialview01'>1kcs</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF ANTIBODY PC282 IN COMPLEX WITH PS1 PEPTIDE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KCS is a [ | + | 1KCS is a [[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=1KCS OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11859128 11859128] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: peptide antigen complex (antibody/peptide)]] | [[Category: peptide antigen complex (antibody/peptide)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:15:38 2008'' |
Revision as of 10:15, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ANTIBODY PC282 IN COMPLEX WITH PS1 PEPTIDE
Overview
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
1KCS is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
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