1jto

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(New page: 200px<br /> <applet load="1jto" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jto, resolution 2.5&Aring;" /> '''Degenerate interface...)
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'''Degenerate interfaces in antigen-antibody complexes'''<br />
'''Degenerate interfaces in antigen-antibody complexes'''<br />
==Overview==
==Overview==
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In most of the work dealing with the analysis of protein-protein, interfaces, a single X-ray structure is available or selected, and, implicitly it is assumed that this structure corresponds to the optimal, complex for this pair of proteins. However, we have found a degenerate, interface in a high-affinity antibody-antigen complex: the two independent, complexes of the camel variable domain antibody fragment cAb-Lys3 and its, antigen hen egg white lysozyme present in the asymmetric unit of our, crystals show a difference in relative orientation between antibody and, antigen, leading to important differences at the protein-protein, interface. A third cAb-Lys3-hen lysozyme complex in a different crystal, form adopts yet another relative orientation. Our results show that, protein-protein interface characteristics can vary significantly between, different specimens of the same high-affinity antibody-protein antigen, complex. Consideration should be given to this type of observation when, trying to establish general protein-protein interface characteristics.
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In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.
==About this Structure==
==About this Structure==
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1JTO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JTO OCA].
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1JTO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] and [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JTO OCA].
==Reference==
==Reference==
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[[Category: Maes, D.]]
[[Category: Maes, D.]]
[[Category: Muyldermans, S.]]
[[Category: Muyldermans, S.]]
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[[Category: Transue, T.R.]]
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[[Category: Transue, T R.]]
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
[[Category: binding]]
[[Category: binding]]
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[[Category: vhh]]
[[Category: vhh]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:34:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:36 2008''

Revision as of 11:26, 21 February 2008


1jto, resolution 2.5Å

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Degenerate interfaces in antigen-antibody complexes

Overview

In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.

About this Structure

1JTO is a Protein complex structure of sequences from Camelus dromedarius and Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Degenerate interfaces in antigen-antibody complexes., Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L, J Mol Biol. 2001 Oct 26;313(3):473-8. PMID:11676532

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