Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/14256
Title: X-ray crystallography of fission yeast RNG2
Authors: WANG CHERN HOE
Keywords: calponin-homology, CH, Rng2, yeast cell-division protein structure
Issue Date: 26-Oct-2004
Source: WANG CHERN HOE (2004-10-26). X-ray crystallography of fission yeast RNG2. ScholarBank@NUS Repository.
Abstract: Schizosaccharomyces pombe Rng2 is an IQGAP protein essential for the assembly of an actomyosin ring during cytokinesis. Rng2 contains an amino-terminal calponin-homology (CH) domain, eleven 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 the third report from actin-binding proteins that contain a single CH domain (the structures of calponin and EB1 have been reported previously). The 2.21 ?? resolution crystal structure of the amino-terminal 189 residues of Rng2 determined using Br- and Hg-derivatives includes 39 residues (150-189) carboxyl-terminal to the CH domain that resembles 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. It wraps around the stretch of residues that would be equivalent to the proposed actin-binding site ABS1 and ABS2 from dystrophin. Another feature revealed by comparing the two derivatives is the presence of two loop conformations between Tyr92-Arg99.
URI: http://scholarbank.nus.edu.sg/handle/10635/14256
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