View source for 4nko


==Crystal structure of engineered anti-EE scFv antibody fragment==
<StructureSection load='4nko' size='340' side='right'caption='[[4nko]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nko]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NKO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.496&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nko OCA], [https://pdbe.org/4nko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nko RCSB], [https://www.ebi.ac.uk/pdbsum/4nko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nko ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein crystallization is dependent upon, and sensitive to, the intermolecular contacts that assist in ordering proteins into a three-dimensional lattice. Here we used protein engineering and mutagenesis to affect the crystallization of single chain antibody fragments (scFvs) that recognize the EE epitope (EYMPME) with high affinity. These hypercrystallizable scFvs are under development to assist difficult proteins, such as membrane proteins, in forming crystals, by acting as crystallization chaperones. Guided by analyses of intermolecular crystal lattice contacts, two second-generation anti-EE scFvs were produced, which bind to proteins with installed EE tags. Surprisingly, although noncomplementarity determining region (CDR) lattice residues from the parent scFv framework remained unchanged through the processes of protein engineering and rational design, crystal lattices of the derivative scFvs differ. Comparison of energy calculations and the experimentally-determined lattice interactions for this basis set provides insight into the complexity of the forces driving crystal lattice choice and demonstrates the availability of multiple well-ordered surface features in our scFvs capable of forming versatile crystal contacts. Proteins 2014. (c) 2014 Wiley Periodicals, Inc.

Effects of protein engineering and rational mutagenesis on crystal lattice of single chain antibody fragments.,Kalyoncu S, Hyun J, Pai JC, Johnson JL, Entzminger K, Jain A, Heaner DP Jr, Morales IA, Truskett TM, Maynard JA, Lieberman RL Proteins. 2014 Feb 26. doi: 10.1002/prot.24542. PMID:24615866<ref>PMID:24615866</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4nko" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Etzminger K]]
[[Category: Heaner Jr D]]
[[Category: Hyun J]]
[[Category: Jain A]]
[[Category: Johnson JL]]
[[Category: Kalyoncu S]]
[[Category: Lieberman RL]]
[[Category: Maynard JA]]
[[Category: Molares IA]]
[[Category: Pai JC]]
[[Category: Truskett TM]]