1ad9

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(New page: 200px<br /> <applet load="1ad9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ad9, resolution 2.80&Aring;" /> '''IGG-FAB FRAGMENT OF...)
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Revision as of 07:18, 18 November 2007


1ad9, resolution 2.80Å

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IGG-FAB FRAGMENT OF ENGINEERED HUMAN MONOCLONAL ANTIBODY CTM01

Overview

The crystal structures of two pairs of Fab fragments have been determined., The pairs comprise both a murine and an engineered human form, each, derived from the antitumor antibodies A5B7 and CTM01. Although antigen, specificity is maintained within the pairs, antigen affinity varies. A, comparison of the hypervariable loops for each pair of antibodies shows, their structure has been well maintained in grafting, supporting the, canonical loop model. Detailed structural analysis of the binding sites, and domain arrangements for these antibodies suggests the differences in, antigen affinity observed are likely to be due to inherent flexibility of, the hypervariable loops and movements at the VL:VH domain interface. The, four structures provide the first opportunity to study in detail the, effects of protein engineering on specific antibodies.

About this Structure

1AD9 is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine antitumor antibodies and their engineered human constructs., Banfield MJ, King DJ, Mountain A, Brady RL, Proteins. 1997 Oct;29(2):161-71. PMID:9329081

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