1jtt: Difference between revisions

Revision as of 14:26, 21 February 2008

Degenerate interfaces in antigen-antibody complexes

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:26:44 2008

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OCA

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-[[Image:1jtt.gif|left|200px]]<br />
+[[Image:1jtt.gif|left|200px]]<br /><applet load="1jtt" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1jtt" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1jtt, resolution 2.1&Aring;" />
 '''Degenerate interfaces in antigen-antibody complexes'''<br />
 ==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.
+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==
-JTT 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] with NA and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1JTT OCA].
+JTT 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] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1JTT OCA].
 ==Reference==
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 [[Category: Maes, D.]]
 [[Category: Muyldermans, S.]]
-[[Category: Transue, T.R.]]
+[[Category: Transue, T R.]]
 [[Category: Wyns, L.]]
 [[Category: FMT]]
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 [[Category: vhh]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:34:18 2007''
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