PDBsum entry: 1ees

Structural protein

PDB-id: 1ees

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

178 a.a. *

46 a.a. *

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1ees

Name:

Structural protein

Title:

Solution structure of cdc42hs complexed with a peptide derived from p-21 activated kinase, nmr, 20 structures

Structure:

Gtp-binding protein. Chain: a. Fragment: amino acids 1-178. Synonym: cdc42hs. Engineered: yes. P21-activated kinase. Chain: b. Fragment: amino acids 65-108. Synonym: mpak-3.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: placenta. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. House mouse. Organism_taxid: 10090.

UniProt:

Chain A: P60953 (CDC42_HUMAN)

Seq:	191 a.a.
Struc:	178 a.a.*

Chain B: Q61036 (PAK3_MOUSE)

Seq:

Struc:

Seq:

Struc:

Seq:

559 a.a.

Struc:

46 a.a.*

Key:	PfamA domain
Secondary structure	CATH domain

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme class:

Chain B: E.C.2.7.11.1   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

ATP + a protein = ADP + a phosphoprotein

Resolution:

not givenÅ

NMR structure:

20 models

Authors:

D.Gizachew,W.Guo,K.C.Chohan,M.J.Sutcliffe,R.E.Oswald

Key ref:

D.Gizachew et al. (2000). Structure of the complex of Cdc42Hs with a peptide derived from P-21 activated kinase.. Biochemistry, 39, 3963-3971. [PubMed id: 10747784] [DOI: 10.1021/bi992646d]

Date:

02-Feb-00

Release date:

29-Mar-00

Related entries:

1aje
cdc42 from human, nmr, 20 structures
1cf4
cdc42 from human complexed with ack, nmr, 20 structures
1cee
cdc42 from human complexed with wasp, nmr, 20 structures

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Clefts

Surface

Key reference

DOI no: 10.1021/bi992646d

Biochemistry 39:3963-3971 (2000)

PubMed id: 10747784

Structure of the complex of Cdc42Hs with a peptide derived from P-21 activated kinase.

D.Gizachew, W.Guo, K.K.Chohan, M.J.Sutcliffe, R.E.Oswald.

ABSTRACT

Cdc42Hs is a member of the Ras superfamily of GTPases and initiates a cascade that begins with the activation of several kinases, including p21-activated kinase (PAK). We have previously used a 46 amino acid fragment of PAK (PBD46) to define the binding surface on Cdc42Hs [Guo et al. (1998) Biochemistry 37, 14030-14037]. Here we describe the three-dimensional solution structure of the Cdc42Hs. GMPPCP-PBD46 complex. Heteronuclear NMR methods were used to assign resonances in the complex, and approximately 2400 distance and dihedral restraints were used to calculate a set of 20 structures using a combination of distance geometry, simulated annealing, and chemical shift and Ramachandran refinement. The overall structure of Cdc42Hs in the complex differs from the uncomplexed structure in two major aspects: (1) the first alpha helix is reoriented to accommodate the binding of the peptide and (2) the regions corresponding to switch I and switch II are less disordered. As suggested by our previous work (Guo et al., 1998) and similar to the complex between Cdc42Hs and fACK [Mott et al. (1999) Nature 399, 384-388], PBD46 forms an intermolecular beta-sheet with beta2 of Cdc42Hs and contacts both switch I and switch II. The extensive binding surface between PBD46 and Cdc42Hs can account for both the high affinity of the complex and the inhibition by PBD46 of GTP hydrolysis.