Please use this identifier to cite or link to this item: https://doi.org/10.1107/S0907444904012983
Title: Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2
Authors: Wang, C.-H.
Balasubramanian, M.K. 
Dokland, T.
Issue Date: Aug-2004
Citation: Wang, C.-H., Balasubramanian, M.K., Dokland, T. (2004-08). Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2. Acta Crystallographica Section D: Biological Crystallography 60 (8) : 1396-1403. ScholarBank@NUS Repository. https://doi.org/10.1107/S0907444904012983
Abstract: Schizosaccharomyces pombe Rng2 is an IQGAP protein that is essential for the assembly of an actomyosin ring during cytokinesis. Rng2 contains an amino-terminal calponin-homology (CH) domain, 11 IQ repeats and a RasGAP-homology domain. CH domains are known mainly for their ability to bind F-actin, although they have other ligands in vivo and there are only few examples of actin-binding single CH domains. The structures of several CH domains have already been reported, but this is only the third report of an actin-binding protein that contains a single CH domain (the structures of calponin and EB1 have been reported previously). The 2.21 Å resolution crystal structure of the amino-terminal 190 residues of Rng2 from Br- and Hg-derivatives includes 40 residues (150-190) carboxyl-terminal to the CH domain that resemble neither the extended conformation seen in utrophin, nor the compact conformation seen in fimbrin, although residues 154-160 form an unstructured coil which adopts a substructure similar to dystrophin residues 240-246 in the carboxyl-terminal portion of the CH2 domain. This region wraps around the stretch of residues that would be equivalent to the proposed actin-binding site ABS1 and ABS2 from dystrophin. This distinctive feature is absent from previously published CH-domain structures. Another feature revealed by comparing the two derivatives is the presence of two loop conformations between Tyr92 and Arg99. © 2004 International Union of Crystallography.
Source Title: Acta Crystallographica Section D: Biological Crystallography
URI: http://scholarbank.nus.edu.sg/handle/10635/130424
ISSN: 09074449
DOI: 10.1107/S0907444904012983
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

8
checked on Aug 13, 2018

WEB OF SCIENCETM
Citations

7
checked on Aug 13, 2018

Page view(s)

14
checked on Jun 28, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.