1lp1: Difference between revisions
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[[Image:1lp1.jpg|left|200px]] | [[Image:1lp1.jpg|left|200px]] | ||
'''Protein Z in complex with an in vitro selected affibody''' | {{Structure | ||
|PDB= 1lp1 |SIZE=350|CAPTION= <scene name='initialview01'>1lp1</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Protein Z in complex with an in vitro selected affibody''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LP1 is a [ | 1LP1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LP1 OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for recognition by an in vitro evolved affibody., Hogbom M, Eklund M, Nygren PA, Nordlund P, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3191-6. Epub 2003 Feb 25. PMID:[http:// | Structural basis for recognition by an in vitro evolved affibody., Hogbom M, Eklund M, Nygren PA, Nordlund P, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3191-6. Epub 2003 Feb 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12604795 12604795] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
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[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:34 2008'' | ||
Revision as of 13:33, 20 March 2008
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Protein Z in complex with an in vitro selected affibody
OverviewOverview
The broad binding repertoire of antibodies has permitted their use in a wide range of applications. However, some uses of antibodies are precluded due to limitations in the efficiency of antibody generation. In vitro evolved binding proteins, selected from combinatorial libraries generated around various alternative structural scaffolds, are promising alternatives to antibodies. We have solved the crystal structure of a complex of an all alpha-helical in vitro selected binding protein (affibody) bound to protein Z, an IgG Fc-binding domain derived from staphylococcal protein A. The structure of the complex reveals an extended and complementary binding surface with similar properties to protein-antibody interactions. The surface region of protein Z recognized by the affibody is strikingly similar to the one used for IgG(1) Fc binding, suggesting that this surface contains potential hot-spots for binding. The implications of the selected affibody binding-mode for its application as a universal binding protein are discussed.
About this StructureAbout this Structure
1LP1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for recognition by an in vitro evolved affibody., Hogbom M, Eklund M, Nygren PA, Nordlund P, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3191-6. Epub 2003 Feb 25. PMID:12604795
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