4gla
From Proteopedia
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- | + | ==OBody NL8 bound to hen egg-white lysozyme== | |
- | + | <StructureSection load='4gla' size='340' side='right' caption='[[4gla]], [[Resolution|resolution]] 2.75Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[4gla]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51768 Atcc 51768] and [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GLA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GLA FirstGlance]. <br> | |
- | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4glv|4glv]], [[4gn3|4gn3]], [[4gn4|4gn4]], [[4gn5|4gn5]]</td></tr> |
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aspS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 ATCC 51768])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=4gla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gla OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gla RCSB], [http://www.ebi.ac.uk/pdbsum/4gla PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> | [[http://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The OB-fold is a small, versatile single-domain protein binding module that occurs in all forms of life, where it binds protein, carbohydrate, nucleic acid and small-molecule ligands. We have exploited this natural plasticity to engineer a new class of non-immunoglobulin alternatives to antibodies with unique structural and biophysical characteristics. We present here the engineering of the OB-fold anticodon recognition domain from aspartyl tRNA synthetase taken from the thermophile Pyrobaculum aerophilum. For this single-domain scaffold we have coined the term OBody. Starting from a naive combinatorial library, we engineered an OBody with 3 nM affinity for hen egg-white lysozyme, by optimising the affinity of a naive OBody 11,700-fold over several affinity maturation steps, using phage display. At each maturation step a crystal structure of the engineered OBody in complex with hen egg-white lysozyme was determined, showing binding elements in atomic detail. These structures have given us an unprecedented insight into the directed evolution of affinity for a single antigen on the molecular scale. The engineered OBodies retain the high thermal stability of the parental OB-fold despite mutation of up to 22% of their residues. They can be expressed in soluble form and also purified from bacteria at high yields. They also lack disulfide bonds. These data demonstrate the potential of OBodies as a new scaffold for the engineering of specific binding reagents and provide a platform for further development of future OBody-based applications. | ||
+ | |||
+ | Tracking Molecular Recognition at the Atomic Level with a New Protein Scaffold Based on the OB-Fold.,Steemson JD, Baake M, Rakonjac J, Arcus VL, Liddament MT PLoS One. 2014 Jan 20;9(1):e86050. doi: 10.1371/journal.pone.0086050. eCollection, 2014 Jan 20. PMID:24465865<ref>PMID:24465865</ref> | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | == | + | ==See Also== |
- | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Atcc 51768]] | [[Category: Atcc 51768]] | ||
[[Category: Chick]] | [[Category: Chick]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
- | [[Category: Steemson, J D | + | [[Category: Steemson, J D]] |
[[Category: Beta barrel]] | [[Category: Beta barrel]] | ||
[[Category: Engineered binding protein]] | [[Category: Engineered binding protein]] |
Revision as of 01:14, 25 December 2014
OBody NL8 bound to hen egg-white lysozyme
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