271:
are all commonly used to purify, immobilize or detect immunoglobulins. Each of these immunoglobulin-binding proteins has a different antibody binding profile in terms of the portion of the antibody that is recognized and the species and type of antibodies it will bind.
250:
forms of protein G. This recombinant protein G, either labeled with a fluorophore or a single-stranded DNA strand, was used as a replacement for secondary antibodies in immunofluorescence and super-resolution imaging.
233:
but with differing binding specificities. It is a ~60-kDA (65 kDA for strain G148 and 58 kDa for strain C40) cell surface protein that has found application in purifying antibodies through its binding to the
414:
Schlichthaerle, Thomas; Ganji, Mahipal; Auer, Alexander; Wade, Orsolya Kimbu; Jungmann, Ralf (2018). "Bacterial-derived antibody binders as small adapters for DNA-PAINT microscopy".
632:
103:
340:). Many previously insoluble domains have become soluble with the fusion of the GB1 domain. The domain is 56 residues (approx 8kDa) long. On
281:
152:
239:
123:
246:, but because serum albumin is a major contaminant of antibody sources, the albumin binding site has been removed from
287:
of the protein G B1 domain demonstrates that, as earlier results suggested, this protein initiates folding via a
235:
111:
626:
107:
583:"Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases"
488:
324:
The last nucleation residue, Y3, assists in forming the central part of the β-sheet resulting in a
457:
652:
614:
563:
514:
449:
441:
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98:
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90:
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218:
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226:
461:
52:
304:
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In addition to protein G, other immunoglobulin-binding bacterial proteins such as
64:
500:
311:
264:
202:
16:
Immunoglobulin-binding protein expressed in group C and G Streptococcal bacteria
549:
477:"Folding pathway of the b1 domain of protein G explored by multiscale modeling"
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296:
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288:
168:
445:
353:
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20:
618:
567:
518:
453:
427:
599:
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341:
173:
59:
375:"Streptococcal protein G. Gene structure and protein binding properties"
336:
to keep other domains in solution during experiments in solution (e.g.
243:
222:
344:
gels the GB1 domain runs at roughly 13.5kDa despite being only 8kDa.
118:
299:
followed by small adjustments. The folding events are as follows:
534:"An efficient system for small protein expression and refolding"
80:
47:
332:
The protein G B1 domain (aka. GB1) is often used as part of a
337:
373:
Sjobring U, Bjorck L, Kastern W, et al. (1991).
307:
is formed, stabilized by residues W43, Y45, and F52.
538:
198:
188:
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147:
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137:
117:
97:
79:
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58:
46:
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33:
28:
581:Hartl MJ, Mayr F, Rethwilm A, Wöhrl BM (2010).
8:
631:: CS1 maint: multiple names: authors list (
310:Residue contacts between residue F30, in an
321:starting from residues L5 and F52, occurs.
180:
71:
608:
598:
557:
508:
435:
390:
532:Cheng, Yuan; Patel, Dinshaw J. (2004).
365:
242:region. The native molecule also binds
624:
134:
25:
7:
475:Kmiecik S, Kolinski A (Feb 2008).
138:Immunoglobulin G-binding protein G
14:
314:, and the β-hairpin strengthen.
276:Folding of protein G, B1 domain
255:Other antibody binding proteins
1:
392:10.1016/S0021-9258(18)52448-0
75:Available protein structures:
501:10.1529/biophysj.107.116095
225:expressed in group C and G
669:
550:10.1016/j.bbrc.2004.03.068
18:
437:21.11116/0000-0003-E68E-A
179:
153:Streptococcus sp. group G
70:
19:Not to be confused with
428:10.1002/cbic.201800743
600:10.1186/1742-4690-7-5
493:2008BpJ....94..726K
229:bacteria much like
317:Nucleation of the
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133:
132:
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124:structure summary
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472:
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422:(8): 1032–1038.
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405:
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326:globular protein
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135:
72:
26:
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24:
17:
12:
11:
5:
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639:
638:
573:
544:(2): 401–405.
524:
467:
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385:(1): 399–405.
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349:
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334:fusion protein
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219:immunoglobulin
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68:
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56:
55:
50:
44:
43:
40:
36:
35:
31:
30:
29:GA-like domain
15:
13:
10:
9:
6:
4:
3:
2:
665:
654:
651:
650:
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634:
628:
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588:
587:Retrovirology
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547:
543:
539:
535:
528:
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520:
516:
511:
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502:
498:
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490:
487:(3): 726–36.
486:
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291:event in the
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227:streptococcal
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37:
32:
27:
22:
627:cite journal
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409:
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331:
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258:
214:
213:
416:ChemBioChem
379:J Biol Chem
293:hydrophobic
265:protein A/G
248:recombinant
193:Swiss-model
143:Identifiers
34:Identifiers
360:References
289:nucleation
285:simulation
189:Structures
184:Search for
87:structures
481:Biophys J
446:1439-7633
354:GA module
305:β-hairpin
283:ab initio
269:protein L
261:protein A
231:protein A
221:-binding
215:Protein G
65:IPR035152
21:G protein
653:Proteins
647:Category
619:20113504
568:15063772
519:17890394
462:58547594
454:30589198
348:See also
342:SDS-PAGE
297:residues
203:InterPro
148:Organism
104:RCSB PDB
60:InterPro
610:2835651
559:4693640
510:2186257
489:Bibcode
401:1985908
319:β-sheet
312:α-helix
244:albumin
223:protein
199:Domains
169:UniProt
53:PF17573
617:
607:
566:
556:
517:
507:
460:
452:
444:
399:
217:is an
174:P06654
160:Symbol
119:PDBsum
93:
83:
39:Symbol
593:: 5.
458:S2CID
295:core
633:link
615:PMID
564:PMID
515:PMID
450:PMID
442:ISSN
397:PMID
267:and
238:and
112:PDBj
108:PDBe
91:ECOD
81:Pfam
48:Pfam
605:PMC
595:doi
554:PMC
546:doi
542:317
505:PMC
497:doi
432:hdl
424:doi
387:doi
383:266
338:NMR
280:An
236:Fab
163:spg
99:PDB
649::
629:}}
625:{{
613:.
603:.
589:.
585:.
562:.
552:.
540:.
536:.
513:.
503:.
495:.
485:94
483:.
479:.
456:.
448:.
440:.
430:.
420:20
418:.
395:.
381:.
377:.
303:a
263:,
240:Fc
110:;
106:;
89:/
635:)
621:.
597::
591:7
570:.
548::
521:.
499::
491::
464:.
434::
426::
403:.
389::
328:.
42:?
23:.
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