1nsn

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(New page: 200px<br /> <applet load="1nsn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nsn, resolution 2.8&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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'''THE CRYSTAL STRUCTURE OF ANTIBODY N10-STAPHYLOCOCCAL NUCLEASE COMPLEX AT 2.9 ANGSTROMS RESOLUTION'''<br />
'''THE CRYSTAL STRUCTURE OF ANTIBODY N10-STAPHYLOCOCCAL NUCLEASE COMPLEX AT 2.9 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The three-dimensional structure of the antibody N10 Fab fragment complexed, with staphylococcal nuclease (SNase) has been determined to 2.9 A, resolution. Eighteen residues from six complementarity-determining regions, (CDR) recognize an epitope of five distinct SNase segments with a total of, 17 residues. The overall shape of the antibody-antigen interface is, U-shaped rather than the more or less rectangular interface seen in other, antibody-protein antigen interfaces. Despite the U-shaped interface, the, amount of surface buried in the complex, 828 A2 for SNase and 793 A2 for, N10, is typical of antibody-protein antigen complexes. Contributing to the, shape of the interface is the shortest antibody heavy chain-CDR3 loop, reported to date, which probably allows access of bulk solvent in the, center of the "U" interface. Another unusual feature of the N10 antibody, is the 15 residue antibody light chain-CDR1, a length seen in only three, other reported antibodies. Antibody light chain-CDR1 displays a previously, unobserved conformation in its distal portion. Finally, although some of, the movement observed in the antibody-bound SNase may be due to crystal, contacts, it is clear that some side-chain rearrangements are the result, of antigen-antibody interaction.
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The three-dimensional structure of the antibody N10 Fab fragment complexed with staphylococcal nuclease (SNase) has been determined to 2.9 A resolution. Eighteen residues from six complementarity-determining regions (CDR) recognize an epitope of five distinct SNase segments with a total of 17 residues. The overall shape of the antibody-antigen interface is U-shaped rather than the more or less rectangular interface seen in other antibody-protein antigen interfaces. Despite the U-shaped interface, the amount of surface buried in the complex, 828 A2 for SNase and 793 A2 for N10, is typical of antibody-protein antigen complexes. Contributing to the shape of the interface is the shortest antibody heavy chain-CDR3 loop reported to date, which probably allows access of bulk solvent in the center of the "U" interface. Another unusual feature of the N10 antibody is the 15 residue antibody light chain-CDR1, a length seen in only three other reported antibodies. Antibody light chain-CDR1 displays a previously unobserved conformation in its distal portion. Finally, although some of the movement observed in the antibody-bound SNase may be due to crystal contacts, it is clear that some side-chain rearrangements are the result of antigen-antibody interaction.
==About this Structure==
==About this Structure==
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1NSN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NSN OCA].
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1NSN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSN OCA].
==Reference==
==Reference==
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[[Category: staphylococcal nuclease]]
[[Category: staphylococcal nuclease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:38:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:33 2008''

Revision as of 12:09, 21 February 2008


1nsn, resolution 2.8Å

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THE CRYSTAL STRUCTURE OF ANTIBODY N10-STAPHYLOCOCCAL NUCLEASE COMPLEX AT 2.9 ANGSTROMS RESOLUTION

Overview

The three-dimensional structure of the antibody N10 Fab fragment complexed with staphylococcal nuclease (SNase) has been determined to 2.9 A resolution. Eighteen residues from six complementarity-determining regions (CDR) recognize an epitope of five distinct SNase segments with a total of 17 residues. The overall shape of the antibody-antigen interface is U-shaped rather than the more or less rectangular interface seen in other antibody-protein antigen interfaces. Despite the U-shaped interface, the amount of surface buried in the complex, 828 A2 for SNase and 793 A2 for N10, is typical of antibody-protein antigen complexes. Contributing to the shape of the interface is the shortest antibody heavy chain-CDR3 loop reported to date, which probably allows access of bulk solvent in the center of the "U" interface. Another unusual feature of the N10 antibody is the 15 residue antibody light chain-CDR1, a length seen in only three other reported antibodies. Antibody light chain-CDR1 displays a previously unobserved conformation in its distal portion. Finally, although some of the movement observed in the antibody-bound SNase may be due to crystal contacts, it is clear that some side-chain rearrangements are the result of antigen-antibody interaction.

About this Structure

1NSN is a Protein complex structure of sequences from Mus musculus and Staphylococcus aureus. Active as Micrococcal nuclease, with EC number 3.1.31.1 Full crystallographic information is available from OCA.

Reference

The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9 A resolution., Bossart-Whitaker P, Chang CY, Novotny J, Benjamin DC, Sheriff S, J Mol Biol. 1995 Nov 3;253(4):559-75. PMID:7473734

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