1hkl
From Proteopedia
(New page: 200px<br /> <applet load="1hkl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hkl, resolution 2.68Å" /> '''FREE AND LIGANDED F...) |
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| - | [[Image:1hkl.gif|left|200px]]<br /> | + | [[Image:1hkl.gif|left|200px]]<br /><applet load="1hkl" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hkl" size=" | + | |
caption="1hkl, resolution 2.68Å" /> | caption="1hkl, resolution 2.68Å" /> | ||
'''FREE AND LIGANDED FORM OF AN ESTEROLYTIC CATALYTIC ANTIBODY'''<br /> | '''FREE AND LIGANDED FORM OF AN ESTEROLYTIC CATALYTIC ANTIBODY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the esterase catalytic antibody 48G7 has been | + | The crystal structure of the esterase catalytic antibody 48G7 has been determined in the presence of hapten at 2.0 A resolution and in the absence of hapten at 2.7 A resolution. The root-mean-square difference between the two structures is 0.6 A for the variable domain and 0.7 A for the constant domain. Comparison of the active site shows that no significant changes occur upon hapten binding as main-chain and side-chain displacements are negligible. Complex formation occurs as hapten fits into a pre-formed pocket about 10 A deep. Although 151 water molecules were modeled into the 48G7-hapten structure, none are bound in the active site. Comparison of the 48G7 structures with those of other published ester hydrolysis antibodies illustrates an emerging theme used by esterolytic antibodies in binding their (nitro-)phenyl haptens and in hydrolysing their cognate esters and carbonates: hapten is bound with the aryl end buried deep in the binding pocket, and the phosphonate moiety is responsible for the majority of the binding energy to the antibody-hapten interaction. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HKL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1HKL is a [http://en.wikipedia.org/wiki/Protein_complex 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=1HKL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Patten, P | + | [[Category: Patten, P A.]] |
| - | [[Category: Schultz, P | + | [[Category: Schultz, P G.]] |
| - | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
| - | [[Category: Wang, L | + | [[Category: Wang, L H.]] |
| - | [[Category: Wedemayer, G | + | [[Category: Wedemayer, G J.]] |
[[Category: catalytic antibody]] | [[Category: catalytic antibody]] | ||
[[Category: ester hydrolysis]] | [[Category: ester hydrolysis]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:12 2008'' |
Revision as of 11:02, 21 February 2008
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FREE AND LIGANDED FORM OF AN ESTEROLYTIC CATALYTIC ANTIBODY
Contents |
Overview
The crystal structure of the esterase catalytic antibody 48G7 has been determined in the presence of hapten at 2.0 A resolution and in the absence of hapten at 2.7 A resolution. The root-mean-square difference between the two structures is 0.6 A for the variable domain and 0.7 A for the constant domain. Comparison of the active site shows that no significant changes occur upon hapten binding as main-chain and side-chain displacements are negligible. Complex formation occurs as hapten fits into a pre-formed pocket about 10 A deep. Although 151 water molecules were modeled into the 48G7-hapten structure, none are bound in the active site. Comparison of the 48G7 structures with those of other published ester hydrolysis antibodies illustrates an emerging theme used by esterolytic antibodies in binding their (nitro-)phenyl haptens and in hydrolysing their cognate esters and carbonates: hapten is bound with the aryl end buried deep in the binding pocket, and the phosphonate moiety is responsible for the majority of the binding energy to the antibody-hapten interaction.
Disease
Known disease associated with this structure: Kappa light chain deficiency OMIM:[147200]
About this Structure
1HKL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of the free and liganded form of an esterolytic catalytic antibody., Wedemayer GJ, Wang LH, Patten PA, Schultz PG, Stevens RC, J Mol Biol. 1997 May 2;268(2):390-400. PMID:9159478
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