1ncc: Difference between revisions

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OCA

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-[[Image:1ncc.gif|left|200px]]<br />
-<applet load="1ncc" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ncc, resolution 2.5&Aring;" />
-'''CRYSTAL STRUCTURES OF TWO MUTANT NEURAMINIDASE-ANTIBODY COMPLEXES WITH AMINO ACID SUBSTITUTIONS IN THE INTERFACE'''<br />
-==Overview==
+==CRYSTAL STRUCTURES OF TWO MUTANT NEURAMINIDASE-ANTIBODY COMPLEXES WITH AMINO ACID SUBSTITUTIONS IN THE INTERFACE==
-The site on influenza virus N9 neuraminidase recognized by NC41 monoclonal, antibody comprises 19 amino acid residues that are in direct contact with, 17 residues on the antibody. Single sequence changes in some of the, neuraminidase residues in the site markedly reduce antibody binding., However, two mutants have been found within the site, Ile368 to Arg and, Asn329 to Asp selected by antibodies other than NC41, and these mutants, bind NC41 antibody with only slightly reduced affinity. The, three-dimensional structures of the two mutant N9-NC41 antibody complexes, as derived from the wild-type complex are presented. Both structures show, that some amino acid substitutions can be accommodated within an, antigen-antibody interface by local structural rearrangements around the, mutation site. In the Ile368 to Arg mutant complex, the side-chain of, Arg368 is shifted by 2.9 A from its position in the uncomplexed mutant and, a shift of 1.3 A in the position of the light chain residue HisL55 with, respect to the wild-type complex is also observed. In the other mutant, the side-chain of Asp329 appears rotated by 150 degrees around C alpha-C, beta with respect to the uncomplexed mutant, so that the carboxylate group, is moved to the periphery of the antigen-antibody interface. The results, provide a basis for understanding some of the potential structural effects, of somatic hypermutation on antigen-antibody binding in those cases where, the mutation in the antibody occurs at antigen-contacting residues, and, demonstrate again the importance of structural context in evaluating the, effect of amino acid substitutions on protein structure and function.
+<StructureSection load='1ncc' size='340' side='right'caption='[[1ncc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ncc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/tern/Australia/G70C/1975(H11N9)) Influenza A virus (A/tern/Australia/G70C/1975(H11N9))] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NCC 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]] 2.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1ncc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ncc OCA], [https://pdbe.org/1ncc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ncc RCSB], [https://www.ebi.ac.uk/pdbsum/1ncc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ncc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GCAM_MOUSE GCAM_MOUSE]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nc/1ncc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1ncc ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-NCC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Viruses Viruses] with NAG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NCC OCA].
+*[[Antibody 3D structures|Antibody 3D structures]]
+*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
-==Reference==
+*[[3D structures of non-human antibody|3D structures of non-human antibody]]
-Crystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interface., Tulip WR, Varghese JN, Webster RG, Laver WG, Colman PM, J Mol Biol. 1992 Sep 5;227(1):149-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1522584 1522584]
+__TOC__
-[[Category: Exo-alpha-sialidase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Protein complex]]
+[[Category: Colman PM]]
-[[Category: Viruses]]
+[[Category: Tulip WR]]
-[[Category: Colman, P.M.]]
+[[Category: Varghese JN]]
-[[Category: Tulip, W.R.]]
-[[Category: Varghese, J.N.]]
-[[Category: CA]]
-[[Category: NAG]]
-[[Category: hydrolase(o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:38:00 2007''