3hfm

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(New page: 200px<br /> <applet load="3hfm" size="450" color="white" frame="true" align="right" spinBox="true" caption="3hfm, resolution 3.0&Aring;" /> '''STRUCTURE OF AN ANTI...)
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'''STRUCTURE OF AN ANTIBODY-ANTIGEN COMPLEX. CRYSTAL STRUCTURE OF THE HY/HEL-10 FAB-LYSOZYME COMPLEX'''<br />
'''STRUCTURE OF AN ANTIBODY-ANTIGEN COMPLEX. CRYSTAL STRUCTURE OF THE HY/HEL-10 FAB-LYSOZYME COMPLEX'''<br />
==Overview==
==Overview==
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The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and, hen egg white lysozyme has been determined to a nominal resolution of 3.0, A. The antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of residues from four different regions of the linear sequence., It consists of the exposed residues of an alpha-helix together with, surrounding amino acids. The epitope crosses the active-site cleft and, includes a tryptophan located within this cleft. The combining site of the, antibody is mostly flat with a protuberance made up of two tyrosines that, penetrate the cleft. All six complementarity-determining regions of the, Fab contribute at least one residue to the binding; one residue from the, framework is also in contact with the lysozyme. The contacting residues on, the antibody contain a disproportionate number of aromatic side chains., The antibody-antigen contact mainly involves hydrogen bonds and van der, Waals interactions; there is one ion-pair interaction but it is weak.
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The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined to a nominal resolution of 3.0 A. The antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of residues from four different regions of the linear sequence. It consists of the exposed residues of an alpha-helix together with surrounding amino acids. The epitope crosses the active-site cleft and includes a tryptophan located within this cleft. The combining site of the antibody is mostly flat with a protuberance made up of two tyrosines that penetrate the cleft. All six complementarity-determining regions of the Fab contribute at least one residue to the binding; one residue from the framework is also in contact with the lysozyme. The contacting residues on the antibody contain a disproportionate number of aromatic side chains. The antibody-antigen contact mainly involves hydrogen bonds and van der Waals interactions; there is one ion-pair interaction but it is weak.
==About this Structure==
==About this Structure==
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3HFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The following page contains interesting information on the relation of 3HFM with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb21_1.html Antibodies]]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3HFM OCA].
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3HFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The following page contains interesting information on the relation of 3HFM with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb21_1.html Antibodies]]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HFM OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davies, D.R.]]
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[[Category: Davies, D R.]]
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[[Category: Padlan, E.A.]]
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[[Category: Padlan, E A.]]
[[Category: complex(antibody-antigen)]]
[[Category: complex(antibody-antigen)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:10:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:42 2008''

Revision as of 17:09, 21 February 2008


3hfm, resolution 3.0Å

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STRUCTURE OF AN ANTIBODY-ANTIGEN COMPLEX. CRYSTAL STRUCTURE OF THE HY/HEL-10 FAB-LYSOZYME COMPLEX

Overview

The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined to a nominal resolution of 3.0 A. The antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of residues from four different regions of the linear sequence. It consists of the exposed residues of an alpha-helix together with surrounding amino acids. The epitope crosses the active-site cleft and includes a tryptophan located within this cleft. The combining site of the antibody is mostly flat with a protuberance made up of two tyrosines that penetrate the cleft. All six complementarity-determining regions of the Fab contribute at least one residue to the binding; one residue from the framework is also in contact with the lysozyme. The contacting residues on the antibody contain a disproportionate number of aromatic side chains. The antibody-antigen contact mainly involves hydrogen bonds and van der Waals interactions; there is one ion-pair interaction but it is weak.

About this Structure

3HFM is a Single protein structure of sequence from Gallus gallus and Mus musculus. The following page contains interesting information on the relation of 3HFM with [Antibodies]. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complex., Padlan EA, Silverton EW, Sheriff S, Cohen GH, Smith-Gill SJ, Davies DR, Proc Natl Acad Sci U S A. 1989 Aug;86(15):5938-42. PMID:2762305

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