Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

The chaperone Î±B-crystallin uses different interfaces to capture an amorphous and an amyloid client.

Mainz A, Peschek J, Stavropoulou M, Back KC, Bardiaux B, Asami S, Prade E, Peters C, Weinkauf S, Buchner J, Reif B

Small heat-shock proteins, including Î±B-crystallin (Î±B), play an important part in protein homeostasis, because their ATP-independent chaperone activity inhibits uncontrolled protein aggregation. Mechanistic details of human Î±B, particularly in its client-bound state, have been elusive so far, owing to the high molecular weight and the heterogeneity of these complexes. Here we provide structural insights into this highly dynamic assembly and ... [more]

Nat. Struct. Mol. Biol. Nov. 01, 2015; 22(11);898-905 [Pubmed: 26458046]

Throughput

Low Throughput

Additional Notes

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
CRYAB CRYAB	Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Fu L (2003)	Low	-	BioGRID	-
CRYAB CRYAB	Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Yamamoto S (2014)	Low	-	BioGRID	-
CRYAB CRYAB	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Bagneris C (2009)	Low	-	BioGRID	723883
CRYAB CRYAB	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Braun N (2011)	Low	-	BioGRID	724052
CRYAB CRYAB	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Jehle S (2010)	Low	-	BioGRID	723762
CRYAB CRYAB	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Rajagopal P (2015)	Low	-	BioGRID	1520788
CRYAB CRYAB	FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.	Murugesan R (2008)	Low	-	BioGRID	-
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Arbach H (2017)	Low	-	BioGRID	2515658
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Braun N (2011)	Low	-	BioGRID	724053
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Fujii N (2008)	Low	-	BioGRID	-
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Jovcevski B (2018)	Low	-	BioGRID	2600559
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Liu L (2006)	Low	-	BioGRID	722333
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Michiel M (2009)	Low	-	BioGRID	723088
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Nourazaran M (2023)	Low	-	BioGRID	-
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Santhoshkumar P (2006)	Low	-	BioGRID	-
CRYAB CRYAB	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Selig EE (2020)	Low	-	BioGRID	-
CRYAB CRYAB	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	DeGrado-Warren J (2008)	Low	-	BioGRID	-
CRYAB CRYAB	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Fu L (2002)	Low	-	BioGRID	303579
CRYAB CRYAB	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Fu L (2003)	Low	-	BioGRID	722962
CRYAB CRYAB	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Rolland T (2014)	High	-	BioGRID	-
CRYAB CRYAB	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Sugiyama Y (2000)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

CRYAB

Gene Ontology Biological Process

Gene Ontology Molecular Function

identical protein binding [IPI]protein binding [IPI]protein homodimerization activity [IPI]unfolded protein binding [IPI]

Gene Ontology Cellular Component