PDBsum entry 2vzc

Cell adhesion

PDB id: 2vzc

Contents

Protein chain

127 a.a. *

Ligands

TRS

GOL

MRD

MPD

Waters ×279

* Residue conservation analysis

PDB id:

2vzc

Name:

Cell adhesion

Title:

Crystal structure of thE C-terminal calponin homology domain of alpha parvin

Structure:

Alpha-parvin. Chain: a, b. Fragment: c-terminal calponin homology domain, residues 242-372. Synonym: calponin-like integrin-linked kinase-binding protein, ch- ilkbp, matrix-remodeling-associated protein 2, actopaxin. Engineered: yes

Source:

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

Resolution:

1.05Å R-factor: 0.144 R-free: 0.159

Authors:

S.Lorenz,I.Vakonakis,E.D.Lowe,I.D.Campbell,M.E.M.Noble,M.K.Hoellerer

Key ref:

S.Lorenz et al. (2008). Structural analysis of the interactions between paxillin LD motifs and alpha-parvin. Structure, 16, 1521-1531. PubMed id: 18940607 DOI: 10.1016/j.str.2008.08.007

Date:

31-Jul-08 Release date: 28-Oct-08

Protein chains

Q9NVD7  (PARVA_HUMAN) -  Alpha-parvin from Homo sapiens

Seq: 372 a.a.

Struc: 127 a.a.

DOI no: 10.1016/j.str.2008.08.007

Structure 16:1521-1531 (2008)

PubMed id: 18940607

Structural analysis of the interactions between paxillin LD motifs and alpha-parvin.

S.Lorenz, I.Vakonakis, E.D.Lowe, I.D.Campbell, M.E.Noble, M.K.Hoellerer.

ABSTRACT

The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs that interact with a variety of focal adhesion proteins, such as alpha-parvin. Here, we report the first crystal structure of the C-terminal calponin homology domain (CH(C)) of alpha-parvin at 1.05 A resolution and show that it is able to bind all the LD motifs, with some selectivity for LD1, LD2, and LD4. Cocrystal structures with these LD motifs reveal the molecular details of their interactions with a common binding site on alpha-parvin-CH(C), which is located at the rim of the canonical fold and includes part of the inter-CH domain linker. Surprisingly, this binding site can accommodate LD motifs in two antiparallel orientations. Taken together, these results reveal an unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell.

Selected figure(s)

Figure 4.
Figure 4. Cocrystal Structure of α-Parvin-CH[C] with Paxillin LD1
Superposition of the ribbon representations of α-parvin-CH[C] in blue and its complex with the LD1 peptide in gold and green, respectively. Secondary structural elements are indicated.

Figure 5.
Figure 5. PRE Experiment with Spin-Labeled LD1
(A) Details of the ^1H-^15N HSQC spectra of 230 μM ^15N-enriched α-parvin-CH[C] and 250 μM PROXYL-labeled LD1 peptide in the absence (left) and presence (right) of 5 mM ascorbate. The latter serves to reduce the spin label, thereby eliminating PRE effects. The binding orientation of LD1 seen in the crystal structure is denoted “forward.”
(B) Ribbon representation of α-parvin-CH[C] in gold and LD1 in green. The position of α-parvin residues 257 and 370 are highlighted in blue and red, respectively.

The above figures are reprinted from an Open Access publication published by Cell Press: Structure (2008, 16, 1521-1531) copyright 2008.

Figures were selected by an automated process.