1h8s
From Proteopedia
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[[Category: anti-ampicillin antibodies]] | [[Category: anti-ampicillin antibodies]] | ||
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Revision as of 13:27, 30 October 2007
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THREE-DIMENSIONAL STRUCTURE OF ANTI-AMPICILLIN SINGLE CHAIN FV FRAGMENT COMPLEXED WITH THE HAPTEN.
Overview
Single-chain Fv (scFv) antibody libraries were constructed from mice, immunized with an ampicillin-bovine serum albumin conjugate. Several, antibodies with specificity for intact ampicillin were selected by phage, display and characterized. The antibody scFv fragment aL2 binds to intact, ampicillin and shows no detectable cross-reactivity with hydrolyzed, ampicillin. We determined the X-ray structures of two crystal forms of, w.t. aL2, which differ mainly in the side-chain conformation of Trp H109, (according to a new consensus nomenclature Kabat residue number H95) in, the extremely short (three residues) CDR H3 and the presence or absence of, a well-resolved molecule of 2-methyl-pentane-2,4-diol in the bottom of the, binding pocket. Attempts to co-crystallize aL2 with its antigen or to, ... [(full description)]
About this Structure
1H8S is a [Single protein] structure of sequence from [Mouse e 010090] with SO4 and AIC as [ligands]. Structure known Active Site: AIC. Full crystallographic information is available from [OCA].
Reference
Selection, characterization and x-ray structure of anti-ampicillin single-chain Fv fragments from phage-displayed murine antibody libraries., Burmester J, Spinelli S, Pugliese L, Krebber A, Honegger A, Jung S, Schimmele B, Cambillau C, Pluckthun A, J Mol Biol. 2001 Jun 8;309(3):671-85. PMID:11397088
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