Please use this identifier to cite or link to this item: https://doi.org/10.1107/S0907444904012983
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dc.titleStructure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2
dc.contributor.authorWang, C.-H.
dc.contributor.authorBalasubramanian, M.K.
dc.contributor.authorDokland, T.
dc.date.accessioned2016-11-16T11:05:49Z
dc.date.available2016-11-16T11:05:49Z
dc.date.issued2004-08
dc.identifier.citationWang, 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
dc.identifier.issn09074449
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/130424
dc.description.abstractSchizosaccharomyces 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1107/S0907444904012983
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1107/S0907444904012983
dc.description.sourcetitleActa Crystallographica Section D: Biological Crystallography
dc.description.volume60
dc.description.issue8
dc.description.page1396-1403
dc.description.codenABCRE
dc.identifier.isiut000222791700007
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