1a4k
From Proteopedia
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|PDB= 1a4k |SIZE=350|CAPTION= <scene name='initialview01'>1a4k</scene>, resolution 2.4Å | |PDB= 1a4k |SIZE=350|CAPTION= <scene name='initialview01'>1a4k</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=FRA:[4-(4-ACETYLAMINO-PHENYL)-3,5-DIOXO-4-AZA-TRICYCLO[5.2.2.0+2,6]UNDEC-1-YLCARBAMOYLOXY]-ACETIC+ACID'>FRA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4k OCA], [http://www.ebi.ac.uk/pdbsum/1a4k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a4k RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding interactions that control the relative geometries of the bound substrates and electronic distribution in the dienophile. A single somatic mutation, serine-91 of the light chain to valine, is largely responsible for the increase in affinity and catalytic activity of the affinity-matured antibody. Structural and functional studies of the germ-line precursor suggest that 39-A11 and related antibodies derive from a family of germ-line genes that have been selected throughout evolution for the ability of the encoded proteins to form a polyspecific combining site. Germ line-encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of structures, may help to expand the binding potential associated with the structural diversity of the primary antibody repertoire. | The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding interactions that control the relative geometries of the bound substrates and electronic distribution in the dienophile. A single somatic mutation, serine-91 of the light chain to valine, is largely responsible for the increase in affinity and catalytic activity of the affinity-matured antibody. Structural and functional studies of the germ-line precursor suggest that 39-A11 and related antibodies derive from a family of germ-line genes that have been selected throughout evolution for the ability of the encoded proteins to form a polyspecific combining site. Germ line-encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of structures, may help to expand the binding potential associated with the structural diversity of the primary antibody repertoire. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Kappa light chain deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147200 147200]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Spiller, B W.]] | [[Category: Spiller, B W.]] | ||
[[Category: Stevens, R C.]] | [[Category: Stevens, R C.]] | ||
| - | [[Category: CD]] | ||
| - | [[Category: FRA]] | ||
[[Category: antibody]] | [[Category: antibody]] | ||
[[Category: catalytic antibody]] | [[Category: catalytic antibody]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:04 2008'' |
Revision as of 15:33, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIELS ALDER CATALYTIC ANTIBODY WITH TRANSITION STATE ANALOGUE
Overview
The three-dimensional structure of an antibody (39-A11) that catalyzes a Diels-Alder reaction has been determined. The structure suggests that the antibody catalyzes this pericyclic reaction through a combination of packing and hydrogen-bonding interactions that control the relative geometries of the bound substrates and electronic distribution in the dienophile. A single somatic mutation, serine-91 of the light chain to valine, is largely responsible for the increase in affinity and catalytic activity of the affinity-matured antibody. Structural and functional studies of the germ-line precursor suggest that 39-A11 and related antibodies derive from a family of germ-line genes that have been selected throughout evolution for the ability of the encoded proteins to form a polyspecific combining site. Germ line-encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of structures, may help to expand the binding potential associated with the structural diversity of the primary antibody repertoire.
About this Structure
1A4K is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Immunological origins of binding and catalysis in a Diels-Alderase antibody., Romesberg FE, Spiller B, Schultz PG, Stevens RC, Science. 1998 Mar 20;279(5358):1929-33. PMID:9506942
Page seeded by OCA on Sun Mar 30 18:33:04 2008
