1fdl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1fdl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdl, resolution 2.5&Aring;" /> '''CRYSTALLOGRAPHIC REF...)
Line 1: Line 1:
-
[[Image:1fdl.gif|left|200px]]<br />
+
[[Image:1fdl.gif|left|200px]]<br /><applet load="1fdl" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1fdl" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1fdl, resolution 2.5&Aring;" />
caption="1fdl, resolution 2.5&Aring;" />
'''CRYSTALLOGRAPHIC REFINEMENT OF THE THREE-DIMENSIONAL STRUCTURE OF THE FAB D1.3-LYSOZYME COMPLEX AT 2.5-ANGSTROMS RESOLUTION'''<br />
'''CRYSTALLOGRAPHIC REFINEMENT OF THE THREE-DIMENSIONAL STRUCTURE OF THE FAB D1.3-LYSOZYME COMPLEX AT 2.5-ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
-
The three-dimensional crystal structure of the complex between the Fab, from the monoclonal anti-lysozyme antibody D1.3 and the antigen, hen egg, white lysozyme, has been refined by crystallographic techniques using, x-ray intensity data to 2.5-A resolution. The antibody contacts the, antigen with residues from all its complementarity determining regions., Antigen residues 18-27 and 117-125 form a discontinuous antigenic, determinant making hydrogen bonds and van der Waals interactions with the, antibody. Water molecules at or near the antigen-antibody interface, mediate some contacts between antigen and antibody. The fine specificity, of antibody D1.3, which does not bind (K alpha less than 10(5) M-1) avian, lysozymes where Gln121 in the amino acid sequence is occupied by His, can, be explained on the basis of the refined model.
+
The three-dimensional crystal structure of the complex between the Fab from the monoclonal anti-lysozyme antibody D1.3 and the antigen, hen egg white lysozyme, has been refined by crystallographic techniques using x-ray intensity data to 2.5-A resolution. The antibody contacts the antigen with residues from all its complementarity determining regions. Antigen residues 18-27 and 117-125 form a discontinuous antigenic determinant making hydrogen bonds and van der Waals interactions with the antibody. Water molecules at or near the antigen-antibody interface mediate some contacts between antigen and antibody. The fine specificity of antibody D1.3, which does not bind (K alpha less than 10(5) M-1) avian lysozymes where Gln121 in the amino acid sequence is occupied by His, can be explained on the basis of the refined model.
==About this Structure==
==About this Structure==
-
1FDL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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 1FDL 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=1FDL OCA].
+
1FDL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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 1FDL 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=1FDL OCA].
==Reference==
==Reference==
Line 17: Line 16:
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Fischmann, T.O.]]
+
[[Category: Fischmann, T O.]]
-
[[Category: Poljak, R.J.]]
+
[[Category: Poljak, R J.]]
[[Category: complex (antibody-antigen)]]
[[Category: complex (antibody-antigen)]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 08:59:58 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:35 2008''

Revision as of 10:37, 21 February 2008


1fdl, resolution 2.5Å

Drag the structure with the mouse to rotate

CRYSTALLOGRAPHIC REFINEMENT OF THE THREE-DIMENSIONAL STRUCTURE OF THE FAB D1.3-LYSOZYME COMPLEX AT 2.5-ANGSTROMS RESOLUTION

Overview

The three-dimensional crystal structure of the complex between the Fab from the monoclonal anti-lysozyme antibody D1.3 and the antigen, hen egg white lysozyme, has been refined by crystallographic techniques using x-ray intensity data to 2.5-A resolution. The antibody contacts the antigen with residues from all its complementarity determining regions. Antigen residues 18-27 and 117-125 form a discontinuous antigenic determinant making hydrogen bonds and van der Waals interactions with the antibody. Water molecules at or near the antigen-antibody interface mediate some contacts between antigen and antibody. The fine specificity of antibody D1.3, which does not bind (K alpha less than 10(5) M-1) avian lysozymes where Gln121 in the amino acid sequence is occupied by His, can be explained on the basis of the refined model.

About this Structure

1FDL is a Protein complex structure of sequences from Gallus gallus and Mus musculus. The following page contains interesting information on the relation of 1FDL with [Antibodies]. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Crystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution., Fischmann TO, Bentley GA, Bhat TN, Boulot G, Mariuzza RA, Phillips SE, Tello D, Poljak RJ, J Biol Chem. 1991 Jul 15;266(20):12915-20. PMID:1712773

Page seeded by OCA on Thu Feb 21 12:37:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools