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1dqq

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(New page: 200px<br /> <applet load="1dqq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dqq, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1dqq.gif|left|200px]]<br />
 
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<applet load="1dqq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dqq, resolution 1.8&Aring;" />
 
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'''CRYSTAL STRUCTURE OF ANTI-LYSOZYME ANTIBODY HYHEL-63'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF ANTI-LYSOZYME ANTIBODY HYHEL-63==
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Antigen-antibody complexes provide useful models for studying the, structure and energetics of protein-protein interactions. We report the, cloning, bacterial expression, and crystallization of the antigen-binding, fragment (Fab) of the anti-hen egg white lysozyme (HEL) antibody HyHEL-63, in both free and antigen-bound forms. The three-dimensional structure of, Fab HyHEL-63 complexed with HEL was determined to 2.0 A resolution, while, the structure of the unbound antibody was determined in two crystal forms, to 1.8 and 2.1 A resolution. In the complex, 19 HyHEL-63 residues from all, six complementarity-determining regions (CDRs) of the antibody contact 21, HEL residues from three discontinuous polypeptide segments of the antigen., The interface also includes 11 bound water molecules, 3 of which are, completely buried in the complex. Comparison of the structures of free and, bound Fab HyHEL-63 reveals that several of the ordered water molecules in, the free antibody-combining site are retained and that additional waters, are added upon complex formation. The interface waters serve to increase, shape and chemical complementarity by filling cavities between the, interacting surfaces and by contributing to the hydrogen bonding network, linking the antigen and antibody. Complementarity is further enhanced by, small (&lt;3 A) movements in the polypeptide backbones of certain antibody, CDR loops, by rearrangements of side chains in the interface, and by a, slight shift in the relative orientation of the V(L) and V(H) domains. The, combining site residues of complexed Fab HyHEL-63 exhibit reduced, temperature factors compared with those of the free Fab, suggesting a loss, in conformational entropy upon binding. To probe the relative contribution, of individual antigen residues to complex stabilization, single alanine, substitutions were introduced in the epitope of HEL recognized by, HyHEL-63, and their effects on antibody affinity were measured using, surface plasmon resonance. In agreement with the crystal structure, HEL, residues at the center of the interface that are buried in the complex, contribute most to the binding energetics (DeltaG(mutant) - DeltaG(wild, type) &gt; 3.0 kcal/mol), whereas the apparent contributions of, solvent-accessible residues at the periphery are much less pronounced, (&lt;1.5 kcal/mol). In the latter case, the mutations may be partially, compensated by local rearrangements in solvent structure that help, preserve shape complementarity and the interface hydrogen bonding network.
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<StructureSection load='1dqq' size='340' side='right'caption='[[1dqq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dqq]] is a 4 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=1DQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQQ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqq OCA], [https://pdbe.org/1dqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqq RCSB], [https://www.ebi.ac.uk/pdbsum/1dqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dqq ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DQQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DQQ OCA].
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Three-dimensional structures of the free and antigen-bound Fab from monoclonal antilysozyme antibody HyHEL-63(,)., Li Y, Li H, Smith-Gill SJ, Mariuzza RA, Biochemistry. 2000 May 30;39(21):6296-309. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10828942 10828942]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Li H]]
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[[Category: Li, H.]]
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[[Category: Mariuzza RA]]
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[[Category: Mariuzza, R.A.]]
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[[Category: anti-lysozyme antibody]]
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[[Category: hen egg white lysozyme]]
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[[Category: hyhel-63]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:28:48 2007''
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Current revision

CRYSTAL STRUCTURE OF ANTI-LYSOZYME ANTIBODY HYHEL-63

PDB ID 1dqq

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