THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR

BODE W, WALTER J, HUBER R, Wenzel H, Tschesche H (1984)
EUROPEAN JOURNAL OF BIOCHEMISTRY 144(1): 185-190.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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DOI
Autor*in
BODE, W; WALTER, J; HUBER, R; Wenzel, HerbertUniBi; Tschesche, HaraldUniBi
Einrichtung
Fakultät für Chemie > Biochemie I
Erscheinungsjahr
1984
Zeitschriftentitel
EUROPEAN JOURNAL OF BIOCHEMISTRY
Band
144
Ausgabe
1
Seite(n)
185-190
ISSN
0014-2956
eISSN
1432-1033
Page URI
https://pub.uni-bielefeld.de/record/1658517

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BODE W, WALTER J, HUBER R, Wenzel H, Tschesche H. THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR. EUROPEAN JOURNAL OF BIOCHEMISTRY. 1984;144(1):185-190.
BODE, W., WALTER, J., HUBER, R., Wenzel, H., & Tschesche, H. (1984). THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR. EUROPEAN JOURNAL OF BIOCHEMISTRY, 144(1), 185-190. https://doi.org/10.1111/j.1432-1033.1984.tb08447.x
BODE, W, WALTER, J, HUBER, R, Wenzel, Herbert, and Tschesche, Harald. 1984. “THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR”. EUROPEAN JOURNAL OF BIOCHEMISTRY 144 (1): 185-190.
BODE, W., WALTER, J., HUBER, R., Wenzel, H., and Tschesche, H. (1984). THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR. EUROPEAN JOURNAL OF BIOCHEMISTRY 144, 185-190.
BODE, W., et al., 1984. THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR. EUROPEAN JOURNAL OF BIOCHEMISTRY, 144(1), p 185-190.
W. BODE, et al., “THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR”, EUROPEAN JOURNAL OF BIOCHEMISTRY, vol. 144, 1984, pp. 185-190.
BODE, W., WALTER, J., HUBER, R., Wenzel, H., Tschesche, H.: THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR. EUROPEAN JOURNAL OF BIOCHEMISTRY. 144, 185-190 (1984).
BODE, W, WALTER, J, HUBER, R, Wenzel, Herbert, and Tschesche, Harald. “THE REFINED 2.2-A (0.22-NM) X-RAY CRYSTAL-STRUCTURE OF THE TERNARY COMPLEX FORMED BY BOVINE TRYPSINOGEN, VALINE-VALINE AND THE ARG15 ANALOG OF BOVINE PANCREATIC TRYPSIN-INHIBITOR”. EUROPEAN JOURNAL OF BIOCHEMISTRY 144.1 (1984): 185-190.

46 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

A genetic selection elucidates structural determinants of arginine versus lysine specificity in trypsin.
Perona JJ, Evnin LB, Craik CS., Gene 137(1), 1993
PMID: 8282194
Natural protein proteinase inhibitors and their interaction with proteinases.
Bode W, Huber R., Eur J Biochem 204(2), 1992
PMID: 1541261
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships.
Bode W, Turk D, Karshikov A., Protein Sci 1(4), 1992
PMID: 1304349
Crystallographic analysis of trypsin-G226A. A specificity pocket mutant of rat trypsin with altered binding and catalysis.
Wilke ME, Higaki JN, Craik CS, Fletterick RJ., J Mol Biol 219(3), 1991
PMID: 2051486
Thermodynamic modeling of internal equilibria involved in the activation of trypsinogen.
Coletta M, Ascenzi P, Bravin L, Amiconi G, Bolognesi M, Guarneri M, Menegatti E., J Biomol Struct Dyn 7(4), 1990
PMID: 2310525
Geometry of binding of the benzamidine- and arginine-based inhibitors N alpha-(2-naphthyl-sulphonyl-glycyl)-DL-p-amidinophenylalanyl-pipe ridine (NAPAP) and (2R,4R)-4-methyl-1-[N alpha-(3-methyl-1,2,3,4-tetrahydro-8- quinolinesulphonyl)-L-arginyl]-2-piperidine carboxylic acid (MQPA) to human alpha-thrombin. X-ray crystallographic determination of the NAPAP-trypsin complex and modeling of NAPAP-thrombin and MQPA-thrombin.
Bode W, Turk D, Stürzebecher J., Eur J Biochem 193(1), 1990
PMID: 2226434
The refined 2.0 A X-ray crystal structure of the complex formed between bovine beta-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes.
Bode W, Greyling HJ, Huber R, Otlewski J, Wilusz T., FEBS Lett 242(2), 1989
PMID: 2914611
Inhibition of serine proteinases by p-carbethoxyphenyl esters of epsilon-guanidino- and epsilon-amino caproic acid: thermodynamic and molecular modeling study.
Menegatti E, Guaneri M, Bolognesi M, Ascenzi P, Amiconi G., J Enzyme Inhib 2(4), 1989
PMID: 2723772
Semisynthesis of Arg15, Glu15, Met15, and Nle15-aprotinin involving enzymatic peptide bond resynthesis.
Beckmann J, Mehlich A, Schröder W, Wenzel HR, Tschesche H., J Protein Chem 8(1), 1989
PMID: 2475133
Geometries of functional group interactions in enzyme-ligand complexes: guides for receptor modelling.
Tintelnot M, Andrews P., J Comput Aided Mol Des 3(1), 1989
PMID: 2715796
The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.
Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J., EMBO J 8(11), 1989
PMID: 2583108
Studies of specificity and catalysis in trypsin by structural analysis of site-directed mutants.
Sprang SR, Fletterick RJ, Gráf L, Rutter WJ, Craik CS., Crit Rev Biotechnol 8(3), 1988
PMID: 3063392
Zymogen activation: effect of peptides sequentially related to the bovine beta-trypsin N-terminus on Kazal inhibitor and benzamidine binding to bovine trypsinogen.
Ascenzi P, Coletta M, Amiconi G, Bolognesi M, Guarneri M, Menegatti E., J Mol Recognit 1(3), 1988
PMID: 3273224
Folding and association of proteins.
Jaenicke R., Prog Biophys Mol Biol 49(2-3), 1987
PMID: 3327098
Binding of the trypsin inhibitor from white mustard (Sinapis alba L.) seeds to bovine beta-trypsin: thermodynamic study.
Menegatti E, Boggian M, Ascenzi P, Luisi PL., J Enzyme Inhib 2(1), 1987
PMID: 3508170
Redesigning trypsin via genetic engineering.
Craik CS, Roczniak S, Sprang S, Fletterick R, Rutter W., J Cell Biochem 33(3), 1987
PMID: 3553217
Similarity and dissimilarity in the stereogeometry of the active sites of thrombin, trypsin, plasmin and glandular kallikrein.
Hijikata-Okunomiya A, Okamoto S, Kikumoto R, Tamao Y, Ohkubo K, Tezuka T, Tonomura S, Matsumoto O., Thromb Res 45(5), 1987
PMID: 2954262
Binding of the Ile-Val and Val-Val effector dipeptides to the binary adducts of bovine trypsinogen with Kunitz and Kazal inhibitors as well as the acylating agent p-nitrophenyl p-guanidinobenzoate. A thermodynamic and kinetic study.
Ascenzi P, Amiconi G, Bolognesi M, Menegatti E, Guarneri M., J Mol Biol 194(4), 1987
PMID: 2443709
The geometries of interacting arginine-carboxyls in proteins.
Singh J, Thornton JM, Snarey M, Campbell SF., FEBS Lett 224(1), 1987
PMID: 3678490
Binding of the bovine pancreatic secretory trypsin inhibitor (Kazal) to bovine serine (pro)enzymes.
Menegatti E, Guarneri M, Bolognesi M, Ascenzi P, Amiconi G., J Mol Biol 198(1), 1987
PMID: 3430603
The interaction of aspartic proteinases with naturally-occurring inhibitors from actinomycetes and Ascaris lumbricoides.
Valler MJ, Kay J, Aoyagi T, Dunn BM., J Enzyme Inhib 1(1), 1985
PMID: 3916913

38 References

Daten bereitgestellt von Europe PubMed Central.

The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen.
Bode W., J. Mol. Biol. 127(4), 1979
PMID: 311834
Preparation and characterization of the active derivative bovine trypsin-kallikrein inhibitor (Kunitz) with the reactive site lysine-15 -- alanine-16 hydrolyzed.
Jering H, Tschesche H., Eur. J. Biochem. 61(2), 1976
PMID: 942916

Huber, Acta Crystallogr. 25(), 1969

AUTHOR UNKNOWN, 0

Jack, Acta Crystallogr. 34(), 1978

AUTHOR UNKNOWN, 0
Energy refinement of hen egg-white lysozyme.
Levitt M., J. Mol. Biol. 82(3), 1974
PMID: 4856348

Huber, Acc. Chem. Res. 11(), 1978
Refined 2 A X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase. Crystallization, structure determination, crystallographic refinement, structure and its comparison with bovine trypsin.
Bode W, Chen Z, Bartels K, Kutzbach C, Schmidt-Kastner G, Bartunik H., J. Mol. Biol. 164(2), 1983
PMID: 6551452

Chothia, Nature (Lond.) 248(), 1974
The interpretation of protein structures: estimation of static accessibility.
Lee B, Richards FM., J. Mol. Biol. 55(3), 1971
PMID: 5551392
Stability and specificity of protein-protein interactions: the case of the trypsin-trypsin inhibitor complexes.
Janin J, Chothia C., J. Mol. Biol. 100(2), 1976
PMID: 943547

AUTHOR UNKNOWN, 0
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