1kfa: Difference between revisions
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[[Image:1kfa.jpg|left|200px]] | [[Image:1kfa.jpg|left|200px]] | ||
'''Crystal structure of Fab fragment complexed with gibberellin A4''' | {{Structure | ||
|PDB= 1kfa |SIZE=350|CAPTION= <scene name='initialview01'>1kfa</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=GA4:GIBBERELLIN A4'>GA4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of Fab fragment complexed with gibberellin A4''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KFA is a [ | 1KFA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFA OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the liganded anti-gibberellin A(4) antibody 4-B8(8)/E9 Fab fragment., Murata T, Fushinobu S, Nakajima M, Asami O, Sassa T, Wakagi T, Yamaguchi I, Biochem Biophys Res Commun. 2002 Apr 26;293(1):489-96. PMID:[http:// | Crystal structure of the liganded anti-gibberellin A(4) antibody 4-B8(8)/E9 Fab fragment., Murata T, Fushinobu S, Nakajima M, Asami O, Sassa T, Wakagi T, Yamaguchi I, Biochem Biophys Res Commun. 2002 Apr 26;293(1):489-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12054627 12054627] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: immunoglobuiln fold]] | [[Category: immunoglobuiln fold]] | ||
''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 12:16:43 2008'' | ||
Revision as of 10:16, 20 March 2008
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| 1kfa, resolution 2.80Å | |||||||||||||
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| Ligands: | GA4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of Fab fragment complexed with gibberellin A4
Overview
Gibberellins, a class of plant hormones, consist of more than 120 members. Only a few of them are recognized by a receptor that remains unknown. The haptenic mouse monoclonal antibody, 4-B8(8)/E9, was generated against gibberellin A(4) (GA(4)) to recognize biologically active GA selectivity, and we attempted to confirm the binding properties between the antibody and GA(4). We carried out an X-ray crystallographic analysis of the 4-B8(8)/E9 Fab fragment complexed with GA(4) at a 2.8 A resolution by using the molecular replacement method. The crystal structure of the Fab fragment showed the typical immunoglobulin fold of the beta-barrel structure which is the common motif of all antibodies. A small hapten-combining site was made up of three heavy chain CDR loops. On the other hand, CDRs of the light chain did not interact directly with GA(4). The C/D rings of the GA(4) molecule were in van der Waals contact mainly with the aromatic side chain of Tyr100AH and Phe100BH of CDR-H3. The 3 beta-hydroxyl and 6 beta-carboxyl groups were, respectively, hydrogen-bonded to the main chain of Ala33H and to the Thr53H heavy chain.
About this Structure
1KFA is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the liganded anti-gibberellin A(4) antibody 4-B8(8)/E9 Fab fragment., Murata T, Fushinobu S, Nakajima M, Asami O, Sassa T, Wakagi T, Yamaguchi I, Biochem Biophys Res Commun. 2002 Apr 26;293(1):489-96. PMID:12054627
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