Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467A

Pflugrath, J.W.; Wiegand, Georg; Huber, Robert; Vértesy, László

doi:10.1016/0022-2836(86)90520-6

Cited by 202 publications

(111 citation statements)

References 16 publications

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“…This is because in the e-amylase inhibitors Haim il and Hoe-46"/A a functionally essential tryptophane is located itl the binding sites with a characteristic Trp-Arg-Tyr-stack [18], PKI3 contains only two tryptophanes which are internal and not exposed on the surface, and consequently cannot be considered as part of the functionally active site, Incubation of PKI3 with PRTK leads to the cleavage of the Ile-75-Ser-'76 peptide bond in PKI3. We have tried to model the structure of the complex between proteinase K and PKI3 with this bond in the active site.…”

Section: Results and Discussionmentioning

confidence: 99%

The three‐dimensional structure of the bifunctional proteinase k/α‐amylase inhibitor from wheat (PKI3) at 2.5 Å resolution

et al. 1991

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Wheat germ contains an inhibitor for proicinase K, called PK13 (M 1 ∼ 19600) which simultaneously inhibits α‐amylase. PK13 was crystallized, space group P21, α = 43.02 (5) Å, n = 65.18 (7) Å, c = 32.33 (4) Å, β = 112.79 (9), X‐ray data were collected to 2.5 Å resolution, the structure solved by molecular replacement on the basis of the atomic coordinates of the homologous Erythrina caffra DE‐3 inhibitor, and refined with simulated annealing techniques with a current R‐factor of 21%. The three‐dimensional structure of PK13 is stabilized by two disulfide bridges and has a central β‐barrel with distorted β‐structure. In analogy to related inhibitors, the binding site for proteinase K is assumed to be located on the surface of the protein (amino acids residues 66–67), although the 75–76 peptide bond is cleaved upon binding.

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Section: Results and Discussionmentioning

confidence: 99%

The three‐dimensional structure of the bifunctional proteinase k/α‐amylase inhibitor from wheat (PKI3) at 2.5 Å resolution

et al. 1991

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“…The global RMSD values in Table 3 imply close similarity among the original solution structure of wild-type Tendamistat [6], the recalculated Tendamistat structure (Table 4), that of [R19L]Tendamistat (Table 2), and the X-ray crystal structure of Tendamistat [8,101. Visual comparisons of the different structures (not shown) confirm this indication.…”

Section: Comparison Of Wild-type Tendamistat With the Mutant Rr19litementioning

confidence: 88%

The nuclear‐magnetic‐resonance solution structure of the mutant α‐amylase inhibitor [R19L]Tendamistat and comparison with wild‐type Tendamistat

O’Connell¹,

Bender²,

Engels

et al. 1994

European Journal of Biochemistry

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The recombinant mutant a-amylase inhibitor [R19L]Tendamistat, with Argl9 replaced by Leu, was prepared and its NMR solution structure determined. Based on complete sequence-specific 'H-NMR assignments, 845 nuclear Overhauser effect upper-distance constraints and 156 dihedral angle constraints were collected using two-dimensional homonuclear 'H-NMR experiments. The structure was calculated with the program DIANA, using the redundant dihedral angle constraints strategy for improved convergence. For restrained energy minimization, the programs FANTOM and AM-BER were used. The wild-type NMR solution structure was similarly recalculated from the previously published input of conformational constraints [Kline, A., Braun, W. & Wuthrich, K. (1988) J. Mol. Biol. 204,. For each protein a group of 20 conformers represents a well-defined solution structure, with average root-mean-square-distance values for the backbone atoms of the individual conformers relative to the mean coordinates of 50 pm. The two structures are nearly identical to each other and to the previously published Tendamistat structures in solution and in crystals. The only significant difference is strictly localized near the single amino acid substitution in the presumed active site -Trpl8-Arg(Leu)-Tyr-, i.e. Leu19 and Tyr2O are more precisely defined in the solution structure of IR19LlTendamistat than the corresponding residues Argl9 and Tyr2O in wild-type Tendamistat.Tendamistat is an a-amylase inhibitor from Streptomyces tendue consisting of a 74-amino-acid polypeptide [ 11, which has played a key role in the development of three-dimensional protein-structure determination by NMR spectroscopy in solution [2]. In fact, although the first NMR structure determinations were those of glucagon [3, 41 and protease inhibitor IIA from bull seminal plasma [5], Tendamistat has been considered by many to be the first true high-resolution

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“…The result of the comparison of the global polypeptide fold of the NMR structures (Kline et al 1986) and of the X-ray structure (Pflugrath et al 1986) of a amylase inhibitor is shown in Fig. 6.…”

Section: A-amylase Inhibitormentioning

confidence: 99%

“…Over several years an extensive set of distance and torsion-angle constraints have been compiled for basic pancreatic trypsin inhibitor (BPTI), the favourite test protein for several experimental and theoretical studies which include the distance (Kline et al 1986) and X-ray techniques (Pflugrath et al 1986). (A) Stereo view of the backbone of four structures calculated by DISMAN from NMR data.…”

Section: Basic Pancreatic Trypsin Inhibitormentioning

confidence: 99%

Distance geometry and related methods for protein structure determination from NMR data

Braun

1987

Quart. Rev. Biophys.

212

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The method of choice to reveal the conformation of protein molecules in atomic detail has been X-ray single-crystal analysis. Since the first structural analysis of diffraction patterns, computer calculations have been an important tool in these studies (Blundell & Johnson, 1976). As is described by Sheldrick (1985), it has been taken for granted that a necessary first step in the determination of a protein structure would be writing computer programs to fit structure factors. In contrast the combined use of the structural analysis of NMR data and computer calculations has been quite limited. An early attempt of such structural calculations was the quantitative determination of mononucleotide conformations in solution using lanthanide ion shifts (Barry et al. 1971).

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Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467A

Cited by 202 publications

References 16 publications

The three‐dimensional structure of the bifunctional proteinase k/α‐amylase inhibitor from wheat (PKI3) at 2.5 Å resolution

The three‐dimensional structure of the bifunctional proteinase k/α‐amylase inhibitor from wheat (PKI3) at 2.5 Å resolution

The nuclear‐magnetic‐resonance solution structure of the mutant α‐amylase inhibitor [R19L]Tendamistat and comparison with wild‐type Tendamistat

Distance geometry and related methods for protein structure determination from NMR data

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