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2
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0003150431
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Introduction to the Protein Inhibitors: X-Ray Crystallography
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A.J. Barrett, G. Salvesen, Elsevier
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(1986)
Proteinase Inhibitors
, pp. 301-336
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Read1
James2
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4
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0040469390
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The 2.5 Å X-Ray Crystal Structure of the Acid-Stable Proteinase Inhibitor from Human Mucous Secretions Analyzed in its Complex with Bovine α-Chymotrypsin
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(1988)
EMBO J
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Grütter1
Fendrich2
Huber3
Bode4
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5
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0024961616
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Structure of the Complex of Streptomyces griseus Proteinase B and Polypeptide Chymotrypsin Inhibitor-1 from Russet Burbank Potato Tubers at 2.1 Å Resolution
-
This paper describes the structure of a new 51-amino acid inhibitor of chymotrypsin, and presents an interesting proposal for the probable structure of a related two-domain inhibitor based on the smaller experimentally determined structure.
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(1989)
J Mol Biol
, vol.205
, pp. 201-225
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Greenblatt1
Ryan2
James3
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6
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0024959382
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The Refined 2.0 Å X-Ray Crystal Structure of the Complex Formed Between Bovine β-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
-
The authors present the structure of a new 29-amino acid inhibitor of trypsin: this suggests that the elongation of the inhibitor's carboxy-terminus could also render it a carboxypeptidase inhibitor; this has since been successfully demonstrated by B Castro and MA Coletti-Previero, (personal communication).
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(1989)
FEBS Lett
, vol.242
, pp. 285-292
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Bode1
Greyling2
Huber3
Otlewski4
Wilusz5
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7
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0025329390
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The Structure of a Complex of Recombinant Hirudin and Human α-Thrombin
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The paper reports concisely the refined high-resolution structure of the thrombin-hirudin complex and, in particular, the detailed interactions of amino- and carboxy-terminal hirudin segments with thrombin-surface sites.
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(1990)
Science
, vol.249
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Rydel1
Ravichandran2
Tulinsky3
Bode4
Huber5
Roitsch6
Fenton7
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9
-
-
0024066065
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The 2.0 Å X-Ray Crystal Structure of Chicken Egg White Cystatin and its Possible Mode of Interaction with Cysteine Proteinases
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This paper presents a structure for cystatin and a docking model of its interaction with papain which, in hindsight, turned out to be essentially correct.
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(1988)
EMBO J
, vol.7
, pp. 2593-2599
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Bode1
Engh2
Musil3
Thiele4
Huber5
Karshikov6
Brzin7
Kos8
Turk9
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10
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0025301658
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The Refined 2.4 Å X-Ray Crystal Structure of Recombinant Human Stefin B in Complex with the Cysteine Proteinase Papain: a Novel Type of Proteinase Inhibitor Interaction
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The authors present the first experimentally determined structure of an inhibitor-cysteine proteinase complex, which confirms the binding mechanism suggested in [9••].
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(1990)
EMBO J
, vol.9
, pp. 1939-1947
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Stubbs1
Laber2
Bode3
Huber4
Jerala5
Lenarcic6
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12
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33947092515
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Structural Basis of the Activation and Action of Trypsin
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(1978)
Acc Chem Res
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Huber1
Bode2
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13
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0024423930
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1-Antitrypsin for Structure and Functions of Serpins
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1-proteinase inhibitors. The binding sites of functional modulators are discussed, and a general explanation of the molecular pathology associated with diverse variants of human serpins is provided.
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(1989)
Biochemistry
, vol.28
, pp. 8951-8966
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Huber1
Carrell2
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14
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0022701771
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Refined 1.2 Å Crystal Structure of the Complex Formed Between Subtilisin Carlsberg and the Inhibitor Eglin C. Molecular Structure of Eglin C and its Detailed Interaction with Subtilisin
-
(1986)
EMBO J
, vol.5
, pp. 813-818
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Bode1
Papamokos2
Musil3
Seemüller4
Fritz5
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16
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0025292406
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Structural Effects Induced by Removal of a Disulfide-Bridge. The X-Ray Structure of the C30A/C51A Mutant of Basic Pancreatic Trypsin Inhibitor at 1.6 Å
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(1990)
Protein Eng
, vol.3
, pp. 591-598
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Eigenbrot1
Randal2
Kossiakoff3
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19
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0023645325
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Protein Structures in Solution by Nuclear Magnetic Resonance and Distance Geometry; the Polypeptide Fold of the Basic Pancreatic Trypsin Inhibitor Determined Using Two Different Algorithms, DISGEO and DISMAN
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(1987)
J Mol Biol
, vol.196
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Wagner1
Braun2
Havel3
Schaumann4
Go5
Wüthrich6
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21
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0024828095
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Nuclear Magnetic Resonance Solution and X-Ray Structures of Squash Trypsin Inhibitor Exhibit the Same Conformation of the Proteinase Binding Loop
-
This paper shows that the conformation of the proteinase-binding loop determined by NMR is extremely similar to that observed in the X-ray structure.
-
(1989)
J Mol Biol
, vol.210
, pp. 649-654
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Holak1
Bode2
Huber3
Otlewski4
Wilusz5
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22
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0025337398
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Role of Arginine 67 in the Stabilization of Chymotrypsin Inhibitor 2: Examination of Amide Proton Exchange Rates and Denaturation Thermodynamics of an Engineered Protein
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−1 to the stability of the whole inhibitor molecule, which forms a single cooperative folding unit.
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(1990)
Biochemistry
, vol.29
, pp. 6264-6269
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Jandu1
Ray2
Brooks3
Leatherbarrow4
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29
-
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0024431034
-
The Refined 1.9 Å Crystal Structure of Human α-Thrombin: Interaction with DPhrProArg Chloromethylketone and Significance of the TyrProProTrp Insertion Segment
-
This paper presents the first three-dimensional X-ray structure of the key coagulating enzyme thrombin. The authors explain the limited reactivity of most ‘small’ serine proteinase inhibitors to thrombin by sterical hindrance with the characteristic thrombin insertion loop around segment Tyr60A-Trp60D.
-
(1989)
EMBO J
, vol.8
, pp. 3467-3475
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Bode1
Mayr2
Baumann3
Huber4
Stone5
Hofsteenge6
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31
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0024817865
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Molecular Dynamics Refinement of a Thermitase-Eglin C Complex at 1.98 Å Resolution and Comparison of Two Crystal Forms that Differ in Calcium Content
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(1989)
J Mol Biol
, vol.210
, pp. 347-367
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Gros1
Betzel2
Dauter3
Wilson4
Hol5
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32
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0024278389
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Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors 2. Sequence-Specific Assignments and Secondary Structure of Reactive Site Modified Turkey Ovomucoid Third Domain
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(1988)
Biochemistry
, vol.27
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Rhyn1
Markley2
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33
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0018781771
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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
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(1979)
J Mol Biol
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Bode1
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34
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0019319082
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Dermasterias imbricata Trypsin 1: an Enzyme which Rapidly Hydrolyzes the Reactive-Site Peptide Bonds of Protein Trypsin Inhibitors
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(1980)
Biochemistry
, vol.19
, pp. 124-131
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Estell1
Laskowski2
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38
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0025276661
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1-Proteinase Inhibitor
-
A structural explanation is presented for observed differences between the inhibitory activities of ovalbumin and the serpins. Further, conformational changes that might occur upon the proteolytic cleavage of functioning serpins are proposed.
-
(1990)
J Mol Biol
, vol.213
, pp. 513-528
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Wright1
Qian2
Huber3
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39
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0025003236
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Crystal Structure of Ovalbumin as a Model for the Reactive Centre of Serpins
-
This paper presents the first structure determined for an uncleaved (non-inhibitory) serpin, which might represent an example of latent-functioning serpins.
-
(1990)
Nature
, vol.347
, pp. 99-102
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Stein1
Leslie2
Finch3
Turnell4
McLaughlin5
Carrell6
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40
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0023700976
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Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites
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(1988)
J Biol Chem
, vol.263
, pp. 16626-16630
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Bruch1
Weiss2
Engel3
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42
-
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0025226070
-
1-Antitrypsin by a Peptide Sequentially Similar to β-Strand S4A
-
1-proteinase inhibitor is inactivated by the insertion of a sequence-related tetradecapeptide. This supports the precept that strand S4A must partially re-enter sheet A in order to render reactive the proteinase-binding loop.
-
(1991)
European Journal of Biochemistry
, vol.194
, pp. 51-56
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Schulze1
Baumann2
Knof3
Jaeger4
Huber5
Laurell6
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44
-
-
0024498476
-
Solution Structure of Recombinant Hirudin and the Lys47 → Glu Mutant: a Nuclear Magnetic Resonance and Hybrid Distance Geometry-Dynamical Simulated Annealing Study
-
A corrected solution structure of hirudin is presented, which suggests that the first two residues and the carboxy-terminal 18-residué tail of hirudin are flexible.
-
(1989)
Biochemistry
, vol.28
, pp. 2601-2617
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-
Folkers1
Clore2
Driscoll3
Dodt4
Köhler5
Gronenborn6
-
45
-
-
0024403533
-
Conformation of Recombinant Desulfatohirudin in Aqueous Solution Determined by Nuclear Magnetic Resonance
-
A solution structure of hirudin is presented, which indicates the absence of a preferred conformation for the first two residues and the carboxy-terminal 17-residue tail.
-
(1989)
Biochemistry
, vol.28
, pp. 4301-4312
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Haruyama1
Wüthrich2
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46
-
-
0024466381
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Quantitative Evaluation of the Contribution of Ionic Interactions to the Formation of the Thrombin-Hirudin Complex
-
The authors evaluate the contributions of single acidic residues of hirudin to thrombin-hirudin binding, on the basis of kinetic measurements made for genetically engineered hirudin forms.
-
(1989)
Biochemistry
, vol.28
, pp. 6857-6863
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Stone1
Dennis2
Hofsteenge3
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50
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0020491126
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Refined Crystal Structure of the Potato Inhibitor Complex of Carboxypeptidase A at 2.5 Å Resolution
-
(1982)
J Mol Biol
, vol.160
, pp. 475-498
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Rees1
Lipscomb2
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51
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0023475020
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Three-Dimensional Structure of Potato Carboxypeptidase Inhibitor in Solution. A Study Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics
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(1987)
Biochemistry
, vol.26
, pp. 8012-8023
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Clore1
Gronenborn2
Nilges3
Ryan4
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