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2b88

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Current revision

Structural basis for molecular recognition in an affibody:affibody complex

Structural highlights

2b88 is a 1 chain structure with sequence from Staphylococcus aureus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q70AB8_STAAU

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Affibody molecules constitute a class of engineered binding proteins based on the 58-residue three-helix bundle Z domain derived from staphylococcal protein A (SPA). Affibody proteins are selected as binders to target proteins by phage display of combinatorial libraries in which typically 13 side-chains on the surface of helices 1 and 2 in the Z domain have been randomized. The Z(Taq):anti-Z(Taq) affibody-affibody complex, consisting of Z(Taq), originally selected as a binder to Taq DNA polymerase, and anti-Z(Taq), selected as binder to Z(Taq), is formed with a dissociation constant K(d) approximately 100 nM. We have determined high-precision solution structures of free Z(Taq) and anti-Z(Taq), and the Z(Taq):anti-Z(Taq) complex under identical experimental conditions (25 degrees C in 50 mM NaCl with 20 mM potassium phosphate buffer at pH 6.4). The complex is formed with helices 1 and 2 of anti-Z(Taq) in perpendicular contact with helices 1 and 2 of Z(Taq). The interaction surface is large ( approximately 1670 A(2)) and unusually non-polar (70 %) compared to other protein-protein complexes. It involves all varied residues on anti-Z(Taq), most corresponding (Taq DNA polymerase binding) side-chains on Z(Taq), and several additional side-chain and backbone contacts. Other notable features include a substantial rearrangement (induced fit) of aromatic side-chains in Z(Taq) upon binding, a close contact between glycine residues in the two subunits that might involve aliphatic glycine Halpha to backbone carbonyl hydrogen bonds, and four hydrogen bonds made by the two guanidinium N(eta)H(2) groups of an arginine side-chain. Comparisons of the present structure with other data for affibody proteins and the Z domain suggest that intrinsic binding properties of the originating SPA surface might be inherited by the affibody binders. A thermodynamic characterization of Z(Taq) and anti-Z(Taq) is presented in an accompanying paper.

Structural basis for molecular recognition in an affibody:affibody complex.,Lendel C, Dogan J, Hard T J Mol Biol. 2006 Jun 23;359(5):1293-304. Epub 2006 May 6. PMID:16750222^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lendel C, Dogan J, Hard T. Structural basis for molecular recognition in an affibody:affibody complex. J Mol Biol. 2006 Jun 23;359(5):1293-304. Epub 2006 May 6. PMID:16750222 doi:10.1016/j.jmb.2006.04.043

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b88"

Categories: Large Structures | Staphylococcus aureus | Dogan J | Hard T | Lendel C

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2b88]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B88 FirstGlance]. <br>
-</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=2b88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b88 OCA], [https://pdbe.org/2b88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b88 RCSB], [https://www.ebi.ac.uk/pdbsum/2b88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b88 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2b88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b88 OCA], [https://pdbe.org/2b88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b88 RCSB], [https://www.ebi.ac.uk/pdbsum/2b88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b88 ProSAT]</span></td></tr>
 </table>
 == Function ==

2b88

From Proteopedia

Current revision

Structural basis for molecular recognition in an affibody:affibody complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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