1LP1

Protein Z in complex with an in vitro selected affibody

Summary for 1LP1

• Entry DOI: 10.2210/pdb1lp1/pdb
• Related: 2spz
• Descriptor: Affibody binding protein Z, Immunoglobulin G binding protein A, SULFATE ION, ... (5 entities in total)
• Functional Keywords: in vitro evolved, protein-protein complex, three-helix bundle, affibody, immune system
• Biological source: Staphylococcus aureus; More
• Cellular location: Secreted, cell wall ; Peptidoglycan-anchor : P38507
• Total number of polymer chains: 2
• Total formula weight: 13504.14

Authors

Hogbom, M.,Eklund, M.,Nygren, P.A.,Nordlund, P. (deposition date: 2002-05-07, release date: 2003-03-18, Last modification date: 2023-10-25)

Primary citation

Hogbom, M.,Eklund, M.,Nygren, P.A.,Nordlund, P.
Structural basis for recognition by an in vitro evolved affibody.
Proc.Natl.Acad.Sci.USA, 100:3191-3196, 2003

PubMed Abstract: 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.

PubMed: 12604795
DOI: 10.1073/pnas.0436100100

Experimental method

X-RAY DIFFRACTION (2.3 Å)