1r0r: Difference between revisions
New page: left|200px<br /><applet load="1r0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r0r, resolution 1.10Å" /> '''1.1 Angstrom Resolut... |
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[[Image:1r0r.jpg|left|200px]]<br /><applet load="1r0r" size=" | [[Image:1r0r.jpg|left|200px]]<br /><applet load="1r0r" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1r0r, resolution 1.10Å" /> | caption="1r0r, resolution 1.10Å" /> | ||
'''1.1 Angstrom Resolution Structure of the Complex Between the Protein Inhibitor, OMTKY3, and the Serine Protease, Subtilisin Carlsberg'''<br /> | '''1.1 Angstrom Resolution Structure of the Complex Between the Protein Inhibitor, OMTKY3, and the Serine Protease, Subtilisin Carlsberg'''<br /> | ||
==Overview== | ==Overview== | ||
Proteins with flexible binding surfaces can interact with numerous binding | Proteins with flexible binding surfaces can interact with numerous binding partners. However, this promiscuity is more difficult to understand in "rigid-body" proteins, whose binding results in little, or no, change in the position of backbone atoms. The binding of Kazal inhibitors to serine proteases is considered a classic case of rigid-body binding, although they bind to a wide range of proteases. We have studied the thermodynamics of binding of the Kazal serine protease inhibitor, turkey ovomucoid third domain (OMTKY3), to the serine protease subtilisin Carlsberg using isothermal titration calorimetry and have determined the crystal structure of the complex at very high resolution (1.1A). Comparison of the binding energetics and structure to other OMTKY3 interactions demonstrates that small changes in the position of side-chains can make significant contributions to the binding thermodynamics, including the enthalpy of binding. These effects emphasize that small, "rigid-body" proteins are still dynamic structures, and these dynamics make contributions to both the enthalpy and entropy of binding interactions. | ||
==About this Structure== | ==About this Structure== | ||
1R0R is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http:// | 1R0R is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] and [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0R OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Subtilisin]] | [[Category: Subtilisin]] | ||
[[Category: Horn, J | [[Category: Horn, J R.]] | ||
[[Category: Murphy, K | [[Category: Murphy, K P.]] | ||
[[Category: Ramaswamy, S.]] | [[Category: Ramaswamy, S.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:48 2008'' | ||
Revision as of 15:45, 21 February 2008
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1.1 Angstrom Resolution Structure of the Complex Between the Protein Inhibitor, OMTKY3, and the Serine Protease, Subtilisin Carlsberg
OverviewOverview
Proteins with flexible binding surfaces can interact with numerous binding partners. However, this promiscuity is more difficult to understand in "rigid-body" proteins, whose binding results in little, or no, change in the position of backbone atoms. The binding of Kazal inhibitors to serine proteases is considered a classic case of rigid-body binding, although they bind to a wide range of proteases. We have studied the thermodynamics of binding of the Kazal serine protease inhibitor, turkey ovomucoid third domain (OMTKY3), to the serine protease subtilisin Carlsberg using isothermal titration calorimetry and have determined the crystal structure of the complex at very high resolution (1.1A). Comparison of the binding energetics and structure to other OMTKY3 interactions demonstrates that small changes in the position of side-chains can make significant contributions to the binding thermodynamics, including the enthalpy of binding. These effects emphasize that small, "rigid-body" proteins are still dynamic structures, and these dynamics make contributions to both the enthalpy and entropy of binding interactions.
About this StructureAbout this Structure
1R0R is a Protein complex structure of sequences from Bacillus licheniformis and Meleagris gallopavo with as ligand. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
ReferenceReference
Structure and energetics of protein-protein interactions: the role of conformational heterogeneity in OMTKY3 binding to serine proteases., Horn JR, Ramaswamy S, Murphy KP, J Mol Biol. 2003 Aug 8;331(2):497-508. PMID:12888355
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