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Document Page 222 site coordinated by invariant Asn171 is also sequestered by the α and γ phosphates. The residue Lys168 is at hydrogen-bond distance from the γ phosphate. The postulated in-line mechanism of phosphotransfer in cAPK [23] can be examined through an analysis of the MnATP and PKI (5–24), Ser substrate peptide and ADP complexes [24]. A comparison between cAPK and IRK structures indicates that Ser versus Tyr specificity is obtained by displacement of the substrate binding site in such a way that the hydroxyl of nucleophiles of both Ser and Tyr fall in the same point in the active site facing corresponding catalytic bases Asp1132 and Asp166 for IRK and cAPK respectively. The purine base of ATP is anchored to the enzyme by three hydrogen bonds, two of them involve the 6amino group and N1 nitrogen, which interact with the backbone atoms of Glu121 and Val123. the 6amino group and N1 nitrogen of the purine base form the hydrogen bonds also in the structure of CK-1 and in the structure of phosphorylase kinase. Yet, in the structure of inactive CDK-2, the purine base forms only one hydrogen bond via its N6 position. While N7 nitrogen interacts directly in cAPK with the side chain of Thr183 in CK-1, this nitrogen interacts directly with Glu55 and Tyr59 via two hydrogen-bonded water molecules and in phosposhorylase kinase via one water molecule. Hence, the N7 nitrogen and its interaction with the enzyme is a region for potential modification of ATP competitive inhibitors. Ribose is held by both enzyme (Glu127 and Glu170) and inhibitor (P-3 Arg). While the side chain of Glu127 interacts with 2'-OH of ribose in cAPK, in CK-1 the 2'-OH interacts via two water molecules with Ser91 and Asp94. In ERK-2, 2'-OH interacts with Asp109. This region has been utilized to design ATP-based specific inhibitors by modifications of the ATP-competitive nonspecific inhibitor staurosporine [25], see Figure 4. In the model cAPK with bound staurosporine inhibitor, the lactam amide group of the inhibitor functions as a bidentate hydrogen bond donor-acceptor Figure 4 Chemical structures of staurosporine inhibitor, left, and CGP52411. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_222.html [4/5/2004 5:07:22 PM]
Document Figure 5 (a) Staurosporine molecule docked in the ATP binding site of PKA. hydrogen bonds anchoring staurosporine molecule in the active site of PKA consists of the 6-amino group and N1 nitrogen and carbonyl of Glu121 and the amide hydrogen atom of Val123. This bidentate hydrogen bond formation has been observed in all complexes of protein kinases and ATP solved so far. (b) Inhibitor of CGP 52411 and ATP docked on the active site of PKA. Residues of Glu127 and Glu170 are also shown and these are not conserved in the EGFR kinase. Page 223 (Figure 5a). This key observation is supported by chemical data of lactam amide derivatives, which provide a plausible model of staurosporine inhibition. This is in the protonated boat-type conformation found to fit in the ATP binding cleft with minimal steric hindrance. In this model, the 4-amino group forms hydrogen bonds with the backbone carbonyl of Glu170 and the carboxylate group of Glu127 of cAPK. A model of the EGFR kinase shows that Glu127 and 170 are replaced by Cys and Arg, respectively (Figure 5b). Replacement of Glu127 by Cys is critical according to the model and explains the several-fold decrease of potency of staurosporine inhibitor toward the EGFR kinase (IC 50=630 nM http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_223.html (1 of 2) [4/5/2004 5:07:30 PM]
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Document Analysis of various HIV-1
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Document Page 54 Table 2) [12,54].
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Document Page 67 Biochemical data s
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Document Chris Tantillo. The work i
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Document Page 72 16. Goldman ME, Nu
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Document 106. Cirino NM, Cameron CE
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Document 122. Marshall WS, Beaton G
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Document dine) and didanosine (dide
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Document Figure 8 Molscript stereo
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Document Page 106 on the same ring
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Document Page 108 mulate during tre
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Document when metals are bound. Fin
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Document cubation of phosphotyrosin
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Document 4 Bradykinin Receptor Anta
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Document Page 127 The des-Arg 9 for
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Document receptor, it has not yet b
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Document Figure 6 Rat and human B2
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Document Figure 9 Composition of te
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Document We determined the structur
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Document Table 1 Inhibition Data fo
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Document Page 166 As predicated, th
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Document References 1. Parks RE Jr.
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Document 17. Ealick SE, Rule SA, Ca
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Document 6 Structural Implications
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Document Page 176 0.43 Å) as the c
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Page 257 and 258: Document 29. Baker ME. Genealogy of
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Document Page 398 with growth hormo
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Document Figure 13 The identified p
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Document 17 Structure and Functiona
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Document Table 1 Approval Indicatio
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Document Page 438 proteins. One pot
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Document II. Type IFNs A great deal
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Document Page 441 sequence of the m
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Document Page 443 that allowed for
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Document Figure 4 Stereo view of IF
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Document Figure 5 Velcro-key model
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Document Figure 6 Proposed receptor
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Document Page 476 nM, respectively.
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Document VI. Conclusion Page 480 It
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Document 21. Both GW, Sleigh MJ, Co
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Document Page 488 against most of t
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Document A. The Canyon Page 491 The
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Document Subsequent studies have sh
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Document Page 495 of the RNA and pr
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Document Figure 4 A ribbon diagram
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Document Figure 5 Some compounds wh
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Document Figure 7 HRV14 VP1 hydroph
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Document Cyclotheonamide A (CtA), 2
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document fragment-based programs, 5
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Document [Human immunodeficiency vi
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Document Kininogen, 119 high molecu
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Document Phosphoglycerate kinase (P
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Document [Protease targets] serinyl
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