PDBsum entry 2xns

Hydrolase/peptide

PDB id: 2xns

Contents

Protein chains

316 a.a.

39 a.a.

Ligands

GDP ×2

SRT ×2

SO4 ×2

Waters ×10

PDB id:

2xns

Name:

Hydrolase/peptide

Title:

Crystal structure of human g alpha i1 bound to a designed helical peptide derived from the goloco motif of rgs14

Structure:

Guanine nucleotide-binding protein g(i) subunit alpha-1. Chain: a, b. Fragment: residues 30-354. Synonym: adenylate cyclase-inhibiting g alpha protein. Engineered: yes. Regulator of g-protein signaling 14. Chain: c, d. Fragment: residues 497-517. Synonym: rgs14.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693. Synthetic: yes. Organism_taxid: 9606

Resolution:

3.41Å R-factor: 0.223 R-free: 0.244

Authors:

D.Bosch,D.W.Sammond,G.L.Butterfoss,M.Machius,D.P.Siderovski,B.Kuhlman

Key ref:

D.W.Sammond et al. (2011). Computational design of the sequence and structure of a protein-binding peptide. J Am Chem Soc, 133, 4190-4192. PubMed id: 21388199

Date:

05-Aug-10 Release date: 08-Jun-11

Protein chains

P63096  (GNAI1_HUMAN) -  Guanine nucleotide-binding protein G(i) subunit alpha-1 from Homo sapiens

Seq: 354 a.a.

Struc: 316 a.a.

Protein chains

O43566  (RGS14_HUMAN) -  Regulator of G-protein signaling 14 from Homo sapiens

Seq: 566 a.a.

Struc: 39 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.6.5.- - ?????

J Am Chem Soc 133:4190-4192 (2011)

PubMed id: 21388199

Computational design of the sequence and structure of a protein-binding peptide.

D.W.Sammond, D.E.Bosch, G.L.Butterfoss, C.Purbeck, M.Machius, D.P.Siderovski, B.Kuhlman.

ABSTRACT

The de novo design of protein-binding peptides is challenging because it requires the identification of both a sequence and a backbone conformation favorable for binding. We used a computational strategy that iterates between structure and sequence optimization to redesign the C-terminal portion of the RGS14 GoLoco motif peptide so that it adopts a new conformation when bound to Gα(i1). An X-ray crystal structure of the redesigned complex closely matches the computational model, with a backbone root-mean-square deviation of 1.1 Å.