3rdm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
<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=3rdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdm RCSB], [http://www.ebi.ac.uk/pdbsum/3rdm PDBsum]</span></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=3rdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdm RCSB], [http://www.ebi.ac.uk/pdbsum/3rdm PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV]] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 08:56, 25 December 2014
Crystal structure of R7-2 streptavidin complexed with biotin/PEGCrystal structure of R7-2 streptavidin complexed with biotin/PEG
Structural highlights
Function[SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMedWe have performed a detailed analysis of streptavidin variants with altered specificity towards desthiobiotin. In addition to changes in key residues which widen the ligand binding pocket and accommodate the more structurally flexible desthiobiotin, the data revealed the role of a key, non-active site mutation at the base of the flexible loop (S52G) which slows dissociation of this ligand by approximately sevenfold. Our data suggest that this mutation results in the loss of a stabilizing contact which keeps this loop open and accessible in the absence of ligand. When this mutation was introduced into the wild-type protein, destabilization of the opened loop conferred a approximately 10-fold decrease in both the on-rate and off-rate for the ligand biotin-4-fluoroscein. A similar effect was observed when this mutation was added to a monomeric form of this protein. Our results provide key insight into the role of the streptavidin flexible loop in ligand binding and maintaining high affinity interactions. Evolved streptavidin mutants reveal key role of loop residue in high-affinity binding.,Magalhaes ML, Czekster CM, Guan R, Malashkevich VN, Almo SC, Levy M Protein Sci. 2011 Jul;20(7):1145-54. doi: 10.1002/pro.642. Epub 2011 May, 12. PMID:21520321[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||