PDBsum entry 3fwv

Chaperone

PDB id

3fwv

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Contents

			Protein chains

					128 a.a. *

			Ligands

					ACE-MET-GLU-GLU- VAL-PHE ×2

			Metals

					_NI ×4

			Waters ×85

* Residue conservation analysis

PDB id:

3fwv

Links

Name:

Chaperone

Title:

Crystal structure of a redesigned tpr protein, t-mod(vmy), in complex with meevf peptide

Structure:

Hsc70/hsp90-organizing protein. Chain: a, b. Fragment: tpr repeats 4-6. Synonym: hop, stress-induced-phosphoprotein 1, sti1, transformation- sensitive protein ief ssp 3521, ny-ren-11 antigen. Engineered: yes. Heat shock protein hsp 90-beta. Chain: c, d. Fragment: c-terminal residues.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: stip1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.

Resolution:

2.20Å

R-factor:

0.187

R-free:

0.244

Authors:

M.E.Jackrel,R.Valverde,L.Regan

Key ref:

M.E.Jackrel et al. (2009). Redesign of a protein-peptide interaction: characterization and applications. Protein Sci, 18, 762-774. PubMed id: 19309728

Date:

19-Jan-09

Release date:

21-Apr-09

PROCHECK

	Headers

	References

Protein chains

P31948 (STIP1_HUMAN) - Stress-induced-phosphoprotein 1 from Homo sapiens

Seq: Struc:

Seq: Struc:					543 a.a. 128 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

	Protein Sci 18:762-774 (2009)
PubMed id: 19309728

Redesign of a protein-peptide interaction: characterization and applications.
M.E.Jackrel, R.Valverde, L.Regan.

ABSTRACT

The design of protein-peptide interactions has a wide array of practical applications and also reveals insight into the basis for molecular recognition. Here, we present the redesign of a tetratricopeptide repeat (TPR) protein scaffold, along with its corresponding peptide ligand. We show that the binding properties of these protein-peptide pairs can be understood, quantitatively, using straightforward chemical considerations. The recognition pairs we have developed are also practically useful for the specific identification of tagged proteins. We demonstrate the facile replacement of these proteins, which we have termed T-Mods (TPR-based recognition module), for antibodies in both detection and purification applications. The new protein-peptide pair has a dissociation constant that is weaker than typical antibody-antigen interactions, yet the recognition pair is highly specific and we have shown that this affinity is sufficient for both Western blotting and affinity purification. Moreover, we demonstrate that this more moderate affinity is actually advantageous for purification applications, because extremely harsh conditions are not required to dissociate the T-Mod-peptide interaction. The results we present are important, not only because they represent a successful application of protein design but also because they help define the properties that should be sought in other scaffolds that are being developed as antibody replacements.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21349882

A.Morin, K.W.Kaufmann, C.Fortenberry, J.M.Harp, L.S.Mizoue, and J.Meiler (2011).
Computational design of an endo-1,4-{beta}-xylanase ligand binding site.

Protein Eng Des Sel, 24, 503-516.

PDB codes:

3mf6 3mf9 3mfa 3mfc

20345907

R.P.Ilagan, E.Rhoades, D.F.Gruber, H.T.Kao, V.A.Pieribone, and L.Regan (2010).
A new bright green-emitting fluorescent protein--engineered monomeric and dimeric forms.

FEBS J, 277, 1967-1978.

20304973

T.Z.Grove, M.Hands, and L.Regan (2010).
Creating novel proteins by combining design and selection.

Protein Eng Des Sel, 23, 449-455.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.