1p2x

<table><tr><td colspan='2'>[[1p2x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P2X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P2X FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNG2 OR SPAC4F8.13C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p2x OCA], [http://pdbe.org/1p2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p2x RCSB], [http://www.ebi.ac.uk/pdbsum/1p2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p2x ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/RNG2_SCHPO RNG2_SCHPO]] Required for cytokinesis. Component of the contractile F-actin ring; required for its construction following assembly of F-actin at the division site.<ref>PMID:9635188</ref>

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== Publication Abstract from PubMed ==

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.

Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2.,Wang CH, Balasubramanian MK, Dokland T Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1396-403. Epub 2004, Jul 21. PMID:15272162<ref>PMID:15272162</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1p2x" style="background-color:#fffaf0;"></div>

[[Category: Cbs 356]]

[[Category: Balasubramanian, M K]]

[[Category: Dokland, T]]

[[Category: Wang, C H]]

[[Category: Helice]]

[[Category: Protein binding]]