PDBsum entry 1g47

Cell adhesion

PDB id: 1g47

Contents

Protein chain

70 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

1g47

Name:

Cell adhesion

Title:

1st lim domain of pinch protein

Structure:

Pinch protein. Chain: a. Fragment: lim1 domain, residues 1-70. Synonym: particularly interesting new cys-his protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: lims1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

25 models

Authors:

A.Velyvis,Y.Yang,C.Wu,J.Qin

Key ref:

A.Velyvis et al. (2001). Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain. J Biol Chem, 276, 4932-4939. PubMed id: 11078733 DOI: 10.1074/jbc.M007632200

Date:

26-Oct-00 Release date: 21-Feb-01

Protein chain

P48059  (LIMS1_HUMAN) -  LIM and senescent cell antigen-like-containing domain protein 1 from Homo sapiens

Seq: 325 a.a.

Struc: 70 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M007632200

J Biol Chem 276:4932-4939 (2001)

PubMed id: 11078733

Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain.

A.Velyvis, Y.Yang, C.Wu, J.Qin.

ABSTRACT

PINCH is a recently identified adaptor protein that comprises an array of five LIM domains. PINCH functions through LIM-mediated protein-protein interactions that are involved in cell adhesion, growth, and differentiation. The LIM1 domain of PINCH interacts with integrin-linked kinase (ILK), thereby mediating focal adhesions via a specific integrin/ILK signaling pathway. We have solved the NMR structure of the PINCH LIM1 domain and characterized its binding to ILK. LIM1 contains two contiguous zinc fingers of the CCHC and CCCH types and adopts a global fold similar to that of functionally distinct LIM domains from cysteine-rich protein and cysteine-rich intestinal protein families with CCHC and CCCC zinc finger types. Gel-filtration and NMR experiments demonstrated a 1:1 complex between PINCH LIM1 and the ankyrin repeat domain of ILK. A chemical shift mapping experiment identified regions in PINCH LIM1 that are important for interaction with ILK. Comparison of surface features between PINCH LIM1 and other functionally different LIM domains indicated that the LIM motif might have a highly variable mode in recognizing various target proteins.

Selected figure(s)

Figure 1.
Fig. 1. Alignment of amino acid sequences of LIM domains with known structures. Alignment was generated with BLAST Version 2.0 (37). Sequence numbering is that of the PINCH protein. Highlighted in black are Zn2+-coordinating residues. The Lasp-1 structure comprises only the first zinc finger, half of the LIM domain. The structure with Protein Data Bank (PDB) code 1cxx is the R122A mutant of qCRP2 LIM2. cCRP1, chicken CRP1.

Figure 3.
Fig. 3. Hydrophobic features of the PINCH LIM1 domain. A, side chain arrangement of hydrophobic core residues of the average minimized structure of PINCH LIM1; B, hydrophobic patch residues near the C terminus of the average minimized structure. The thin ribbon represents the backbone of residues 49-67 ( -sheet 4 and -helix); side chains are shown as sticks.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 4932-4939) copyright 2001.

Figures were selected by an automated process.