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1yqv

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(New page: 200px<br /> <applet load="1yqv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yqv, resolution 1.7&Aring;" /> '''The crystal structur...)
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caption="1yqv, resolution 1.7&Aring;" />
'''The crystal structure of the antibody Fab HyHEL5 complex with lysozyme at 1.7A resolution'''<br />
'''The crystal structure of the antibody Fab HyHEL5 complex with lysozyme at 1.7A resolution'''<br />
==Overview==
==Overview==
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The structure of the complex between hen egg-white lysozyme and the Fab, HyHEL-5 at 2.7 A resolution has previously been reported [Cohen et al., (1996), Acta Cryst. D52, 315-326]. With the availability of recombinant, Fab, the X-ray structure of the complex has been re-evaluated at 1.7 A, resolution. The refined structure has yielded a detailed picture of the, Fab-lysozyme interface, showing the high complementarity of the protein, surfaces as well as several water molecules within the interface that, complete the good fit. The model of the full complex has improved, significantly, yielding an R(work) of 19.5%. With this model, the, structural results can be compared with the results of isothermal, titration calorimetry. An attempt has been made to estimate the changes in, bound waters that accompany complex formation and the difficulties, inherent in using the crystal structures to provide the information, necessary to make this calculation are discussed.
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The structure of the complex between hen egg-white lysozyme and the Fab HyHEL-5 at 2.7 A resolution has previously been reported [Cohen et al. (1996), Acta Cryst. D52, 315-326]. With the availability of recombinant Fab, the X-ray structure of the complex has been re-evaluated at 1.7 A resolution. The refined structure has yielded a detailed picture of the Fab-lysozyme interface, showing the high complementarity of the protein surfaces as well as several water molecules within the interface that complete the good fit. The model of the full complex has improved significantly, yielding an R(work) of 19.5%. With this model, the structural results can be compared with the results of isothermal titration calorimetry. An attempt has been made to estimate the changes in bound waters that accompany complex formation and the difficulties inherent in using the crystal structures to provide the information necessary to make this calculation are discussed.
==About this Structure==
==About this Structure==
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1YQV 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]. This structure superseeds the now removed PDB entries 3HFL and 2HFL. The following page contains interesting information on the relation of 1YQV 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=1YQV OCA].
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1YQV 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]. This structure supersedes the now removed PDB entries 3HFL and 2HFL. The following page contains interesting information on the relation of 1YQV 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=1YQV OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cohen, G.H.]]
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[[Category: Cohen, G H.]]
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[[Category: Davies, D.R.]]
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[[Category: Davies, D R.]]
[[Category: Dyda, F.]]
[[Category: Dyda, F.]]
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[[Category: Padlan, E.A.]]
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[[Category: Padlan, E A.]]
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[[Category: Silverton, E.W.]]
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[[Category: Silverton, E W.]]
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[[Category: Wibbenmeyer, J.A.]]
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[[Category: Wibbenmeyer, J A.]]
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[[Category: Wilson, R.C.]]
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[[Category: Wilson, R C.]]
[[Category: hyhel-5 antibody]]
[[Category: hyhel-5 antibody]]
[[Category: lysozyme]]
[[Category: lysozyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:07:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:11 2008''

Revision as of 14:08, 21 February 2008


1yqv, resolution 1.7Å

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The crystal structure of the antibody Fab HyHEL5 complex with lysozyme at 1.7A resolution

Overview

The structure of the complex between hen egg-white lysozyme and the Fab HyHEL-5 at 2.7 A resolution has previously been reported [Cohen et al. (1996), Acta Cryst. D52, 315-326]. With the availability of recombinant Fab, the X-ray structure of the complex has been re-evaluated at 1.7 A resolution. The refined structure has yielded a detailed picture of the Fab-lysozyme interface, showing the high complementarity of the protein surfaces as well as several water molecules within the interface that complete the good fit. The model of the full complex has improved significantly, yielding an R(work) of 19.5%. With this model, the structural results can be compared with the results of isothermal titration calorimetry. An attempt has been made to estimate the changes in bound waters that accompany complex formation and the difficulties inherent in using the crystal structures to provide the information necessary to make this calculation are discussed.

About this Structure

1YQV is a Single protein structure of sequence from Gallus gallus and Mus musculus. This structure supersedes the now removed PDB entries 3HFL and 2HFL. The following page contains interesting information on the relation of 1YQV with [Antibodies]. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Water molecules in the antibody-antigen interface of the structure of the Fab HyHEL-5-lysozyme complex at 1.7 A resolution: comparison with results from isothermal titration calorimetry., Cohen GH, Silverton EW, Padlan EA, Dyda F, Wibbenmeyer JA, Willson RC, Davies DR, Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):628-33. Epub 2005, Apr 20. PMID:15858274

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