PDBsum entry 2nqc

Immune system

PDB id: 2nqc

Contents

Protein chain

97 a.a. *

Ligands

IMD ×2

GOL ×2

Metals

_NI

Waters ×56

* Residue conservation analysis

PDB id:

2nqc

Name:

Immune system

Title:

Crystal structure of ig-like domain 23 from human filamin c

Structure:

Filamin-c. Chain: a. Fragment: ig-like domain 23. Synonym: gamma-filamin, filamin-2, protein flnc, actin-binding- like protein, abp-l, abp-280-like protein. Engineered: yes

Source:

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

Resolution:

2.05Å R-factor: 0.190 R-free: 0.237

Authors:

L.Sjekloca,R.Pudas,B.Sjoeblom,P.Konarev,O.Carugo,V.Rybin,T.R.Kiema, D.Svergun,J.Ylanne,K.Djinovic-Carugo

Key ref:

L.Sjekloća et al. (2007). Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol, 368, 1011-1023. PubMed id: 17379241 DOI: 10.1016/j.jmb.2007.02.018

Date:

31-Oct-06 Release date: 11-Sep-07

Protein chain

Q14315  (FLNC_HUMAN) -  Filamin-C from Homo sapiens

Seq: 2725 a.a.

Struc: 97 a.a.

DOI no: 10.1016/j.jmb.2007.02.018

J Mol Biol 368:1011-1023 (2007)

PubMed id: 17379241

Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer.

L.Sjekloća, R.Pudas, B.Sjöblom, P.Konarev, O.Carugo, V.Rybin, T.R.Kiema, D.Svergun, J.Ylänne, K.D.Carugo.

ABSTRACT

Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation experiments showed that the filamin C domains 19-21 form elongated monomers in diluted solutions.

Selected figure(s)

Figure 1.
Figure 1. Cartoon representation in stereo of Ig-like domain 23 from filamin C. β-Strand elements are represented in yellow, helical turns in red, and the connecting loops are coloured in green.

Figure 4.
Figure 4. (a) Experimental X-ray scattering pattern from filamin C Ig-like domains 23–24 dimer. Scattering from a typical ab initio model computed by DAMMIN (continuous line, red) and from the three-dimensional model with added linker parts between domains 23 and 24 obtained by BUNCH^8 (broken line, blue). The plot displays the logarithm of the scattering intensity as a function of momentum transfer s = 4π sin(θ)/λ, where 2θ is the scattering angle and λ = 0.15 nm is the X-ray wavelength. The distance distribution function is displayed in the inner window on top right. (b) Ab initio and rigid models of the filamin C Ig-like domains 23–24 dimer. Ab initio models of filamin C Ig-like domain 23–24 dimer superimposed with the rigid body models. The ab initio models obtained by DAMMIN are displayed as gray semitransparent spheres, the models obtained by BUNCH as C^α traces (the two monomers are coloured red and blue, the linkers are green). Top panel, models without symmetry; bottom panel, models with P2 symmetry axis (vertical axis on the bottom left). The right view is rotated clockwise around the horizontal axis. The bar represents the length of 50 Å and is shown at the top left.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 368, 1011-1023) copyright 2007.

Figures were selected by the author.