Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit

EMBO Journal

Volumn 24, Issue 2, 2005, Pages 229-239

  Antcliff, Jennifer F ^a   Haider, Shozeb ^a   Proks, Peter ^a   Sansom, Mark S P ^a   Ashcroft, Frances M ^a,b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

ATP binding; KATP channel; Kir6.2

Indexed keywords

ADENINE; ADENOSINE TRIPHOSPHATE; INWARDLY RECTIFYING POTASSIUM CHANNEL SUBUNIT KIR6.2; LIGAND; PHOSPHATE; TETRAMER;

ANIMAL CELL; ARTICLE; BINDING SITE; CHANNEL GATING; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; MOLECULAR MODEL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; RAT; SITE DIRECTED MUTAGENESIS; XENOPUS LAEVIS;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; ION CHANNEL GATING; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POTASSIUM CHANNELS, INWARDLY RECTIFYING; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA; XENOPUS LAEVIS;

EID: 13444274375     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600487     Document Type: Article

References (45)

1. +-channels by a photoactivatable ATP-analogue in mouse pancreatic beta-cells. Biochim Biophys Acta 1092: 347-349
2. 2+ ions. J Physiol 416: 349-367
3. Brejc K, van Dijk WJ, Klaassen RV, Schuurmans M, van Der Oost J, Smit AB, Sixma TK (2001) Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411: 269-276
4. Capener CE, Proks P, Ashcroft FM, Sansom MS (2003) Filter flexibility in a mammalian K channel: models and simulations of Kir6.2 mutants. Biophys J 84: 2345-2356
5. ATP channel subunits. Neuron 18: 827-838
6. ATP channels. J Gen Physiol 120: 437-446
7. ATP channel subunit Kir6.2. J Physiol 557: 347-354
8. ATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit. Proc Natl Acad Sci USA 95: 13953-13958
9. Dunne MJ, Cosgrove KE, Shepherd RM, Aynsley-Green A, Lindley KJ (2004) Hyperinsulinism in infancy: from basic science to clinical disease. Physiol Rev 84: 239-275
10. Fiser A, Do R, Sali A (2000) Modeling of loops in protein structures. Prot Sci 9: 1753-1773
11. Gloyn AL, Pearson ER, Antcliff JF, Proks P, Bruining GJ, Slingerland AS, Howard N, Srinivasan S, Silva JM, Molnes J, Edghill EL, Frayling TM, Temple IK, Mackay D, Shield JP, Sumnik Z, van Rhijn A, Wales JK, Clark P, German S, Aisenberg J, Ellard S, Njolstad PR, Ashcroft FM, Hattersley AT (2004) Activating mutations in the ATP-sensitive potassium channel subunit Kir6.2 gene are associated with permanent neonatal diabetes. New Engl J Med 350: 1838-1849
12. Goodsell DS, Morris GM, Olson AJ (1996) Automated docking of flexible ligands: applications of AutoDock. J Mol Recog 9: 1-5
13. Gribble FM, Tucker SJ, Ashcroft FM (1997) The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by MgADP and diazoxide. EMBO J 16: 1145-1152
14. + channel Kir6.2. J Physiol 552: 23-34
15. Jones P, Tucker S, Ashcroft FM (2001) Multiple sites of interaction between the intracellular domains of an inwardly-rectifying potassium channel, Kir6.2. FEES Lett 508: 85-89
16. + channel. Biochem Pharm 54: 219-225
17. Kuo A, Gulbis JM, Antcliff JF, Rahman T, Lowe ED, Zimmer J, Cuthbertson J, Ashcroft FM, Ezaki T, Doyle DA (2003) Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300: 1922-1926
18. ATP channel inhibition by ATP. Biophys J 79: 841-852
19. Light PE, Bladen C, Winkfein RJ, Walsh MP, French RJ (2000) Molecular basis of protein kinase C-induced activation of ATP-sensitive potassium channels. Proc Natl Acad Sci USA 97: 9058-9063
20. Lin YW, Jia T, Weinsoft AM, Shyng SL (2003) Stabilization of the activity of ATP-sensitive potassium channels by ion pairs formed between adjacent Kir6.2 subunits. J Gen Physiol 122: 225-237
21. + channel pore. Proc Natl Acad Sci USA 98: 4227-4232
22. 4-mediates closure of pancreatic beta-cell ATP-sensitive potassium channels by interaction with 1 of 4 identical sites. Diabetes 49: 1413-1418
23. Morris AL, MacArthur MW, Hutchinson EG, Thornton JM (1992) Stereochemical quality of protein structure coordinates. Proteins 12: 345-364
24. Nichols CG, Shyng SL, Nestorowicz A, Glaser B, Clement IV JP, Gonzalez G, Aguilar-Bryan L, Permutt MA, Bryan J (1996) Adenosine diphosphate as an intracellular regulator of insulin secretion. Science 272: 1785-1787
25. Nishida M, MacKinnon R (2002) Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 Å resolution. Cell 111: 957-965
26. Proks P, Gribble FM, Adhikari R, Tucker SJ, Ashcroft FM (1999) Involvement of the N-terminus of Kir6.2 in the inhibition of the KATP channel by ATP. J Physiol 514: 19-25
27. ATP channel by ATP. J Physiol 520: 661-669
28. Ribalet B, John SA, Weiss JN (2003) Molecular basis for Kir6.2 channel inhibition by adenine nucleotides. Biophys J 84: 266-276
29. Russel RB, Saqi MA, Sayle RA, Bates PA, Sternberg MJ (1997) Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation. J Mol Biol 269: 423-439
30. Sagen JV, Raeder H, Hathout E, Shehadeh N, Gudmundsson K, Baevre H, Abuelo D, Phornphutkul C, Molnes J, Bell GI, Gloyn AL, Hattersley AT, Molven A, Sovik O, Njolstad PR (2004) Permanent neonatal diabetes due to mutations in KCNJ11 encoding Kir6.2: patient characteristics and initial response to sulfonylurea therapy. Diabetes 53: 2713-2718
31. Sali A, Blundell TL (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815
32. 2 site in the N terminus. J Biol Chem 278: 10500-10505
33. + channels. Prog Biophys Mol Biol 81: 133-176
34. ATP channels by the Kir6.2 subunit. J Gen Physiol 110: 141-153
35. ATP channels. J Gen Physiol 116: 599-608
36. Spruce AE, Standen NB, Stanfield PR (1987) Studies of the unitary properties of adenosine-5′-triphosphate-regulated potassium channels of frog skeletal muscle. J Physiol 382: 213-236
37. 32P]ATP- [γ]4-azidoanilide. Biochim Biophys Res Commun 272: 316-319
38. + channel by 8-Azido-ATP. J Biol Chem 274: 3931-3933
39. Trapp S, Haider S, Jones P, Sansom MSP, Ashcroft FM (2003) Identification of residues contributing to the ATP-binding site of Kir6.2. EMBO J 22: 2903-2912
40. ATP channel gating and implications for channel inhibition by ATP. J Gen Physiol 112: 333-349
41. + channel Kir6.2 revealed by fluorescence resonance energy transfer. Proc Natl Acad Sci USA 101: 76-81
42. Tucker SJ, Ashcroft FM (1999) Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2. J Biol Chem 274: 33393-33397
43. ATP channel inhibition by ATP. EMBO J 17: 3290-3296
44. Tucker SJ, Gribble FM, Zhao C, Trapp S, Ashcroft FM (1997) Truncation of Kir6.2 produces ATP-sensitive K-channels in the absence of the sulphonylurea receptor. Nature 387: 179-183
45. Vaxillaire M, Populaire C, Busiah K, Cave H, Gloyn AL, Hattersley AT, Czernichow P, Froguel P, Polak M (2004) Kir6.2 mutations are a common cause of permanent neonatal diabetes in a large cohort of French patients. Diabetes 53: 2719-2722