1zvh: Difference between revisions

Revision as of 06:55, 29 July 2008

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File:1zvh.png

Template:STRUCTURE 1zvh

Crystal stucture of the VHH domain D2-L24 in complex with hen egg white lysozymeCrystal stucture of the VHH domain D2-L24 in complex with hen egg white lysozyme

Template:ABSTRACT PUBMED 16537393

About this StructureAbout this Structure

1ZVH is a Single protein structure of sequence from Camelus dromedarius and Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies., De Genst E, Silence K, Decanniere K, Conrath K, Loris R, Kinne J, Muyldermans S, Wyns L, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4586-91. Epub 2006 Mar 13. PMID:16537393

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OCA

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-'''Crystal stucture of the VHH domain D2-L24 in complex with hen egg white lysozyme'''
+===Crystal stucture of the VHH domain D2-L24 in complex with hen egg white lysozyme===
-==Overview==
+<!--
-Clefts on protein surfaces are avoided by antigen-combining sites of conventional antibodies, in contrast to heavy-chain antibodies (HCAbs) of camelids that seem to be attracted by enzymes' substrate pockets. The explanation for this pronounced preference of HCAbs was investigated. Eight single domain antigen-binding fragments of HCAbs (VHH) with nanomolar affinities for lysozyme were isolated from three immunized dromedaries. Six of eight VHHs compete with small lysozyme inhibitors. This ratio of active site binders is also found within the VHH pool derived from polyclonal HCAbs purified from the serum of the immunized dromedary. The crystal structures of six VHHs in complex with lysozyme and their interaction surfaces were compared to those of conventional antibodies with the same antigen. The interface sizes of VHH and conventional antibodies to lysozyme are very similar as well as the number and chemical nature of the contacts. The main difference comes from the compact prolate shape of VHH that presents a large convex paratope, predominantly formed by the H3 loop and interacting, although with different structures, into the concave lysozyme substrate-binding pocket. Therefore, a single domain antigen-combining site has a clear structural advantage over a conventional dimeric format for targeting clefts on antigenic surfaces.
+The line below this paragraph, {{ABSTRACT_PUBMED_16537393}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16537393 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16537393}}
 ==About this Structure==
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 [[Category: Immunoglobulin fold]]
 [[Category: Protein-protein heterocomplex]]
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