Source:http://linkedlifedata.com/resource/pubmed/id/15272162
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 8
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pubmed:dateCreated |
2004-7-23
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pubmed:databankReference | |
pubmed:abstractText |
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 A 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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bromine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mercury,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Rng2 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/calponin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1396-403
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:15272162-Binding Sites,
pubmed-meshheading:15272162-Bromine,
pubmed-meshheading:15272162-Calcium-Binding Proteins,
pubmed-meshheading:15272162-Cell Cycle Proteins,
pubmed-meshheading:15272162-Crystallography, X-Ray,
pubmed-meshheading:15272162-GTPase-Activating Proteins,
pubmed-meshheading:15272162-Mercury,
pubmed-meshheading:15272162-Microfilament Proteins,
pubmed-meshheading:15272162-Models, Molecular,
pubmed-meshheading:15272162-Protein Conformation,
pubmed-meshheading:15272162-Schizosaccharomyces,
pubmed-meshheading:15272162-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:15272162-Sequence Homology, Amino Acid
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pubmed:year |
2004
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pubmed:articleTitle |
Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2.
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pubmed:affiliation |
Institute of Molecular and Cell Biology, 61 Biopolis Drive (Proteos), Singapore 138673, Singapore. chernhoe@imcb.a-star.edu.sg
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pubmed:publicationType |
Journal Article
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