1lmk: Difference between revisions
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[[Image:1lmk.gif|left|200px]] | [[Image:1lmk.gif|left|200px]] | ||
'''THE STRUCTURE OF A BIVALENT DIABODY''' | {{Structure | ||
|PDB= 1lmk |SIZE=350|CAPTION= <scene name='initialview01'>1lmk</scene>, resolution 2.6Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= L5MK16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''THE STRUCTURE OF A BIVALENT DIABODY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LMK is a [ | 1LMK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMK OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a diabody, a bivalent antibody fragment., Perisic O, Webb PA, Holliger P, Winter G, Williams RL, Structure. 1994 Dec 15;2(12):1217-26. PMID:[http:// | Crystal structure of a diabody, a bivalent antibody fragment., Perisic O, Webb PA, Holliger P, Winter G, Williams RL, Structure. 1994 Dec 15;2(12):1217-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7704531 7704531] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:37 2008'' | ||
Revision as of 10:32, 20 March 2008
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| 1lmk, resolution 2.6Å | |||||||||||||
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| Gene: | L5MK16 (Mus musculus) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE STRUCTURE OF A BIVALENT DIABODY
Overview
BACKGROUND: Diabodies are dimeric antibody fragments. In each polypeptide, a heavy-chain variable domain (VH) is linked to a light-chain variable domain (VL) but unlike single-chain Fv fragments, each antigen-binding site is formed by pairing of one VH and one VL domain from the two different polypeptides. Diabodies thus have two antigen-binding sites, and can be bispecific. Direct structural evidence is lacking for the connections and dimeric interactions between the two polypeptides of the diabody. RESULTS: The 2.6 A resolution structure has been determined for a bivalent diabody with a flexible five-residue polypeptide linker between the (amino-terminal) VH and (carboxy-terminal) VL domains. The asymmetric unit of the crystal consists of four polypeptides comprising two diabodies; for one of these polypeptides the linker can be traced between the VH and VL domains. Within each diabody the two associated VH and VL domains make back-to-back interactions through the VH domains, and there is an extensive VL-VL interface between the two diabodies in the asymmetric unit. CONCLUSIONS: The structure of the diabody is very similar to that which had been predicted by molecular modelling. Diabodies directed against cell-surface antigens should be capable of bringing together two cells, such as in cell-targeted therapy, because the two antigen-binding sites of the diabody are at opposite ends of the molecule and separated by approximately 65 A.
About this Structure
1LMK is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a diabody, a bivalent antibody fragment., Perisic O, Webb PA, Holliger P, Winter G, Williams RL, Structure. 1994 Dec 15;2(12):1217-26. PMID:7704531
Page seeded by OCA on Thu Mar 20 12:32:37 2008
