PDBsum entry 2bzy

Sh3 domain

PDB id: 2bzy

Contents

Protein chains

63 a.a. *

* Residue conservation analysis

PDB id:

2bzy

Name:

Sh3 domain

Title:

Homodimer of crkl-sh3c domain

Structure:

Crk-like protein. Chain: a, b. Fragment: sh3 domain, residues 237-303. Synonym: crkl sh3c. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.50Å R-factor: 0.263 R-free: 0.309

Authors:

M.Harkiolaki,R.J.Gilbert,E.Y.Jones,S.M.Feller

Key ref:

M.Harkiolaki et al. (2006). The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal. Structure, 14, 1741-1753. PubMed id: 17161365 DOI: 10.1016/j.str.2006.09.013

Date:

24-Aug-05 Release date: 28-Sep-06

Protein chains

P46109  (CRKL_HUMAN) -  Crk-like protein from Homo sapiens

Seq: 303 a.a.

Struc: 63 a.a.

DOI no: 10.1016/j.str.2006.09.013

Structure 14:1741-1753 (2006)

PubMed id: 17161365

The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal.

M.Harkiolaki, R.J.Gilbert, E.Y.Jones, S.M.Feller.

ABSTRACT

CRKL plays essential roles in cell signaling. It consists of an N-terminal SH2 domain followed by two SH3 domains. SH2 and SH3N bind to signaling proteins, but the function of the SH3C domain has remained largely enigmatic. We show here that the SH3C of CRKL forms homodimers in protein crystals and in solution. Evidence for dimer formation of full-length CRKL is also presented. In the SH3C dimer, a nuclear export signal (NES) is mostly buried under the domain surface. The same is true for a monomeric SH3C obtained under different crystallization conditions. Interestingly, partial SH3 unfolding, such as occurs upon dimer/monomer transition, produces a fully-accessible NES through translocation of a single beta strand. Our results document the existence of an SH3 domain dimer formed through exchange of the first SH3 domain beta strand and suggest that partial unfolding of the SH3C is important for the relay of information in vivo.

Selected figure(s)

Figure 2.
Figure 2. The CRKL SH3C Dimer
Schematic representation of the CRKL SH3C dimer (A), where the two polypeptide chains are colored green and red, respectively, with all β strands numbered from N to C terminus and a second view of the same structure (B) produced through a 90° clockwise rotation around the x axis of (A). The second orientation (B) is also viewed as a space-filling model (C). (D) C[α] models of the SH3C dimer and superimposed monomers. The two polypeptide chains in the dimer are colored green and red, respectively, while the monomers are in gray. The structures were superimposed in LSQKAB (Kabsch, 1976) with equivalences of core SH3 fold residues across species. Orientation same as in (A).

Figure 6.
Figure 6. Examples of Known SH3 Dimers
Ribbon representations of SH3 fold dimers (partner subunit polypeptide chains in green and red, respectively) of Vav and Grb2 (A) (Nishida et al., 2001), Grap2 (Mona/Gads) (B) (Harkiolaki et al., 2003), KorB-C (C), p47^phox (D) (Delbruck et al., 2002), and Eps8 (E) (Kishan et al., 1997). The yellow circle in (B) represents a crucial divalent metal ion.

The above figures are reprinted by permission from Cell Press: Structure (2006, 14, 1741-1753) copyright 2006.

Figures were selected by an automated process.