1cdk
CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (E.C.2.7.1.37) (PROTEIN KINASE A) COMPLEXED WITH PROTEIN KINASE INHIBITOR PEPTIDE FRAGMENT 5-24 (PKI(5-24) ISOELECTRIC VARIANT CA) AND MN2+ ADENYLYL IMIDODIPHOSPHATE (MNAMP-PNP) AT PH 5.6 AND 7C AND 4CCAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (E.C.2.7.1.37) (PROTEIN KINASE A) COMPLEXED WITH PROTEIN KINASE INHIBITOR PEPTIDE FRAGMENT 5-24 (PKI(5-24) ISOELECTRIC VARIANT CA) AND MN2+ ADENYLYL IMIDODIPHOSPHATE (MNAMP-PNP) AT PH 5.6 AND 7C AND 4C
Template:ABSTRACT PUBMED 8384554
About this StructureAbout this Structure
1cdk is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA.
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ReferenceReference
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- ↑ Bossemeyer D, Engh RA, Kinzel V, Ponstingl H, Huber R. Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J. 1993 Mar;12(3):849-59. PMID:8384554
- ↑ Denessiouk KA, Lehtonen JV, Korpela T, Johnson MS. Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites. Protein Sci. 1998 May;7(5):1136-46. PMID:9605318 doi:10.1002/pro.5560070507
- ↑ Yang J, Cron P, Good VM, Thompson V, Hemmings BA, Barford D. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat Struct Biol. 2002 Dec;9(12):940-4. PMID:12434148 doi:10.1038/nsb870
- ↑ Iakoucheva LM, Radivojac P, Brown CJ, O'Connor TR, Sikes JG, Obradovic Z, Dunker AK. The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res. 2004 Feb 11;32(3):1037-49. Print 2004. PMID:14960716 doi:10.1093/nar/gkh253
- ↑ Desveaux D, Singer AU, Wu AJ, McNulty BC, Musselwhite L, Nimchuk Z, Sondek J, Dangl JL. Type III effector activation via nucleotide binding, phosphorylation, and host target interaction. PLoS Pathog. 2007 Mar;3(3):e48. PMID:17397263 doi:10.1371/journal.ppat.0030048