1mel
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(New page: 200px<br /> <applet load="1mel" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mel, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 07:29, 18 November 2007
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CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN COMPLEX WITH LYSOZYME
Overview
The Camelidae is the only taxonomic family known to possess functional, heavy-chain antibodies, lacking light chains. We report here the 2.5 A, resolution crystal structure of a camel VH in complex with its antigen, lysozyme. Compared to human and mouse VH domains, there are no major, backbone rearrangements in the VH framework. However, the architecture of, the region of VH that interacts with a VL in a conventional FV is, different from any previously seen. Moreover, the CDR1 region, although in, sequence homologous to human CDR1, deviates fundamentally from the, canonical structure. Additionally, one half of the CDR3 contacts the VH, region which in conventional immunoglobulins interacts with a VL whereas, the other half protrudes from the antigen binding site and penetrates, deeply into the active site of lysozyme.
About this Structure
1MEL is a Single protein structure of sequence from Camelus dromedarius and Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme., Desmyter A, Transue TR, Ghahroudi MA, Thi MH, Poortmans F, Hamers R, Muyldermans S, Wyns L, Nat Struct Biol. 1996 Sep;3(9):803-11. PMID:8784355
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