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| | ==A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G== | | ==A NOVEL, HIGHLY STABLE FOLD OF THE IMMUNOGLOBULIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G== |
| - | <StructureSection load='1gb1' size='340' side='right'caption='[[1gb1]], [[NMR_Ensembles_of_Models | 60 NMR models]]' scene=''> | + | <StructureSection load='1gb1' size='340' side='right'caption='[[1gb1]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_griseus"_krainsky_1914 "actinomyces griseus" krainsky 1914]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GB1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gb1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GB1 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gb1|2gb1]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gb1 OCA], [http://pdbe.org/1gb1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gb1 RCSB], [http://www.ebi.ac.uk/pdbsum/1gb1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gb1 ProSAT]</span></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=1gb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gb1 OCA], [https://pdbe.org/1gb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gb1 RCSB], [https://www.ebi.ac.uk/pdbsum/1gb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gb1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG]] Binds to the constant Fc region of IgG with high affinity. | + | [https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces griseus krainsky 1914]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Clore, G M]] | + | [[Category: Streptomyces griseus]] |
| - | [[Category: Gronenborn, A M]] | + | [[Category: Clore GM]] |
| - | [[Category: Immunoglobulin binding protein]] | + | [[Category: Gronenborn AM]] |
| Structural highlights
Function
SPG1_STRSG Binds to the constant Fc region of IgG with high affinity.
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
The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C).
A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.,Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM Science. 1991 Aug 9;253(5020):657-61. PMID:1871600[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gronenborn AM, Filpula DR, Essig NZ, Achari A, Whitlow M, Wingfield PT, Clore GM. A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G. Science. 1991 Aug 9;253(5020):657-61. PMID:1871600
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