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| {{STRUCTURE_2c1o| PDB=2c1o | SCENE= }} | | {{STRUCTURE_2c1o| PDB=2c1o | SCENE= }} |
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| '''ENAIIHIS FAB FRAGMENT IN THE FREE FORM'''
| | ===ENAIIHIS FAB FRAGMENT IN THE FREE FORM=== |
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| ==Overview==
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| Enantioselective antibodies can separate the enantiomers of a chiral compound in a highly specific manner. We have recently reported the cloning and applications of a recombinant Fab-fragment, ENA11His, in the enantioseparation of a drug candidate, finrozole, which contains two chiral centers. Here, the crystal structures of this enantioselective antibody Fab-fragment are determined in the absence of the hapten at a resolution of 2.75 A, and in the presence of the hapten at 2.05 A resolution. The conformation of the protein was found to be similar in both free and complex forms. The hapten molecule was tightly bound in a deep cleft between the light and heavy chains of the Fab-fragment. The complex structure also allowed us to describe the molecular basis for enantioselectivity and to deduce the absolute configurations of all the four different stereoisomers (a-d) of finrozole. The ENA11His antibody fragment selectively binds the SR (a) enantiomer from the racemic mixture of a and d-enantiomers, thus allowing separation from the pharmacologically most active RS enantiomer (d). In particular, Asp95 and Asn35 of the H-chain in the ENA11 His antibody seem to provide this specificity through hydrogen bonding.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16427081}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16427081 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16427081}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Immune system]] | | [[Category: Immune system]] |
| [[Category: Immunoglobulin domain]] | | [[Category: Immunoglobulin domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:06:40 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:00:58 2008'' |
