4znc: Difference between revisions
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==Fc fragment of human IgG in complex with the C domain of staphylococcal protein A mutant - Q9W== | ==Fc fragment of human IgG in complex with the C domain of staphylococcal protein A mutant - Q9W== | ||
<StructureSection load='4znc' size='340' side='right' caption='[[4znc]], [[Resolution|resolution]] 2.28Å' scene=''> | <StructureSection load='4znc' size='340' side='right'caption='[[4znc]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4znc]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZNC FirstGlance]. <br> | <table><tr><td colspan='2'>[[4znc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZNC FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wwi|4wwi]], [[4zmd|4zmd]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wwi|4wwi]], [[4zmd|4zmd]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885]), IGHG3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4znc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4znc OCA], [http://pdbe.org/4znc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4znc RCSB], [http://www.ebi.ac.uk/pdbsum/4znc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4znc ProSAT]</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=4znc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4znc OCA], [http://pdbe.org/4znc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4znc RCSB], [http://www.ebi.ac.uk/pdbsum/4znc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4znc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Deis, L N]] | [[Category: Deis, L N]] | ||
[[Category: Oas, T G]] | [[Category: Oas, T G]] | ||
Revision as of 11:13, 26 June 2019
Fc fragment of human IgG in complex with the C domain of staphylococcal protein A mutant - Q9WFc fragment of human IgG in complex with the C domain of staphylococcal protein A mutant - Q9W
Structural highlights
Publication Abstract from PubMedStaphylococcal protein A (SpA) is an important virulence factor from Staphylococcus aureus responsible for the bacterium's evasion of the host immune system. SpA includes five small three-helix-bundle domains that can each bind with high affinity to many host proteins such as antibodies. The interaction between a SpA domain and the Fc fragment of IgG was partially elucidated previously in the crystal structure 1FC2. Although informative, the previous structure was not properly folded and left many substantial questions unanswered, such as a detailed description of the tertiary structure of SpA domains in complex with Fc and the structural changes that take place upon binding. Here we report the 2.3-A structure of a fully folded SpA domain in complex with Fc. Our structure indicates that there are extensive structural rearrangements necessary for binding Fc, including a general reduction in SpA conformational heterogeneity, freezing out of polyrotameric interfacial residues, and displacement of a SpA side chain by an Fc side chain in a molecular-recognition pocket. Such a loss of conformational heterogeneity upon formation of the protein-protein interface may occur when SpA binds its multiple binding partners. Suppression of conformational heterogeneity may be an important structural paradigm in functionally plastic proteins. Suppression of conformational heterogeneity at a protein-protein interface.,Deis LN, Wu Q, Wang Y, Qi Y, Daniels KG, Zhou P, Oas TG Proc Natl Acad Sci U S A. 2015 Jul 21;112(29):9028-33. doi:, 10.1073/pnas.1424724112. Epub 2015 Jul 8. PMID:26157136[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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