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|Title:||Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2|
|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|
|Appears in Collections:||Staff Publications|
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