1omd

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

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

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

[[http://www.uniprot.org/uniprot/ONCO_RAT ONCO_RAT]] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.

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== Publication Abstract from PubMed ==

The crystal structure of oncomodulin, a 12,000 Mr protein isolated from rat tumours, has been determined by molecular replacement using the carp parvalbumin structure as a starting model. Refinement was performed by cycles of molecular fitting and restrained least-squares, using area-detector intensity data to 1.85 A resolution. For the 5770 reflections in the range 6.0 to 1.85 A, which were used in the refinement, the crystallographic R-factor is 0.166. The refined model includes residues 2 to 108, three Ca2+ and 87 water molecules per oncomodulin molecule. The oncomodulin backbone is closely related to that of parvalbumin; however, some differences are found after a least-squares fit of the two backbones, with root-mean-square (r.m.s.) deviations of 1 to 2 A in residues 2 to 6, 59 to 61 of the CD loop, 87, 90 and 108. The overall r.m.s. deviation of the backbone residues 5 to 108 is 0.62 A. Each of the two Ca2+ atoms that are bound to the CD and EF loops is co-ordinated to seven oxygen atoms, including one water molecule. The third Ca2+ is also seven-co-ordinated, to five oxygen atoms belonging to three different oncomodulin molecules and to two water molecules which form hydrogen bonds to a fourth oncomodulin; thus, this intermolecular Ca2+ and its equivalents interlink the molecules into zigzag layers normal to the b axis with a spacing of b/2 or 32.14 A. No such extensive molecular aggregation has been reported for any of the related Ca-binding regulatory proteins of the troponin-C family studied thus far. The Ca-O distances in all three polyhedra are in the range 2.07 A to 2.64 A, indicating tightly bound Ca polyhedra.

Structure of oncomodulin refined at 1.85 A resolution. An example of extensive molecular aggregation via Ca2+.,Ahmed FR, Przybylska M, Rose DR, Birnbaum GI, Pippy ME, MacManus JP J Mol Biol. 1990 Nov 5;216(1):127-40. PMID:2231727<ref>PMID:2231727</ref>

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

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== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Ahmed, F R]]

[[Category: Birnbaum, G I]]

[[Category: Macmanus, J P]]

[[Category: Pippy, M E]]

[[Category: Przybylska, M]]

[[Category: Rose, D R]]

[[Category: Calcium binding protein]]