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1kcv

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{{STRUCTURE_1kcv| PDB=1kcv | SCENE= }}
{{STRUCTURE_1kcv| PDB=1kcv | SCENE= }}
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'''Crystal structure of antibody pc282'''
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===Crystal structure of antibody pc282===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11859128 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11859128}}
==About this Structure==
==About this Structure==
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[[Category: Anti-peptide antibody]]
[[Category: Anti-peptide antibody]]
[[Category: Fab fragment]]
[[Category: Fab fragment]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:08:41 2008''

Revision as of 07:08, 2 July 2008

Image:1kcv.png

Template:STRUCTURE 1kcv

Crystal structure of antibody pc282

Template:ABSTRACT PUBMED 11859128

About this Structure

1KCV 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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