1c89
From Proteopedia
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- | [[ | + | ==NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA STRUCTURES== |
+ | <StructureSection load='1c89' size='340' side='right' caption='[[1c89]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1c89]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pachycara_brachycephalum Pachycara brachycephalum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C89 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c8a|1c8a]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c89 RCSB], [http://www.ebi.ac.uk/pdbsum/1c89 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The structure of a new antifreeze protein (AFP) variant, RD3, from antarctic eel pout (Rhigophila dearborni) with enhanced activity has been determined for the first time by nuclear magnetic resonance spectroscopy. RD3 comprises a unique translational topology of two homologous type III AFP globular domains, each containing one flat, ice binding plane. The ice binding plane of the N domain is located approximately 3.5 A "behind" that of the C domain. The two ice binding planes are located laterally with an angle of 32 +/- 12 degrees between the planes. These results suggest that the C domain plane of RD3 binds first to the ice [1010] prism plane in the <0001> direction, which induces successive ice binding of the N domain in the <0101> direction. This manner of ice binding caused by the unique structural topology of RD3 is thought to be crucial for the significant enhancement of antifreeze activity, especially at low AFP concentrations. | ||
- | + | NMR analysis of type III antifreeze protein intramolecular dimer. Structural basis for enhanced activity.,Miura K, Ohgiya S, Hoshino T, Nemoto N, Suetake T, Miura A, Spyracopoulos L, Kondo H, Tsuda S J Biol Chem. 2001 Jan 12;276(2):1304-10. PMID:11010977<ref>PMID:11010977</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Antifreeze protein|Antifreeze protein]] | *[[Antifreeze protein|Antifreeze protein]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Pachycara brachycephalum]] | [[Category: Pachycara brachycephalum]] | ||
[[Category: Miura, K.]] | [[Category: Miura, K.]] |
Revision as of 17:02, 20 August 2014
NMR STRUCTURE OF INTRAMOLECULAR DIMER ANTIFREEZE PROTEIN RD3, 40 SA STRUCTURES
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