1ufd
From Proteopedia
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| - | + | ==COMPARATIVE MODELING OF NODULIN 26 FROM GLYCINE MAX.== | |
| + | <StructureSection load='1ufd' size='340' side='right' caption='[[1ufd]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UFD FirstGlance]. <br> | ||
| + | </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=1ufd FirstGlance], [http://www.ebi.ac.uk/pdbsum/1ufd PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A model of the nodulin 26 channel protein has been constructed based on comparative modeling and molecular dynamics simulations. Structural features of the protein indicate a selectivity filter that differs from those of the known structures of Escherichia coli glycerol facilitator and mammalian aquaporin 1. The model structure also reveals important roles of Ser207 and Phe96 in ligand binding and transport. | ||
| - | + | Functional properties of soybean nodulin 26 from a comparative three-dimensional model.,Biswas S FEBS Lett. 2004 Jan 30;558(1-3):39-44. PMID:14759513<ref>PMID:14759513</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
| - | < | + | |
[[Category: Biswas, S]] | [[Category: Biswas, S]] | ||
Revision as of 20:22, 28 September 2014
COMPARATIVE MODELING OF NODULIN 26 FROM GLYCINE MAX.
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