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2zpk

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2zpk, resolution 1.80Å ()
Sites: , and
Ligands:
Non-Standard Residues:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of P20.1 Fab fragment in complex with its antigen peptide

Publication Abstract from PubMed

Biologically important human proteins often require mammalian cell expression for structural studies, presenting technical and economical problems in the production/purification processes. We introduce a novel affinity peptide tagging system that uses a low affinity anti-peptide monoclonal antibody. Concatenation of the short recognition sequence enabled the successful engineering of an 18-residue affinity tag with ideal solution binding kinetics, providing a low-cost purification means when combined with nondenaturing elution by water-miscible organic solvents. Three-dimensional information provides a firm structural basis for the antibody-peptide interaction, opening opportunities for further improvements/modifications.

Novel affinity tag system using structurally defined antibody-tag interaction: application to single-step protein purification., Nogi T, Sangawa T, Tabata S, Nagae M, Tamura-Kawakami K, Beppu A, Hattori M, Yasui N, Takagi J, Protein Sci. 2008 Dec;17(12):2120-6. Epub 2008 Sep 11. PMID:18787202

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2ZPK is a 6 chains structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Novel affinity tag system using structurally defined antibody-tag interaction: application to single-step protein purification., Nogi T, Sangawa T, Tabata S, Nagae M, Tamura-Kawakami K, Beppu A, Hattori M, Yasui N, Takagi J, Protein Sci. 2008 Dec;17(12):2120-6. Epub 2008 Sep 11. PMID:18787202

Page seeded by OCA on Wed Dec 24 11:27:39 2008

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