Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition (Q27647015)

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Language	Label	Description	Also known as
English	Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition	scientific article

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scholarly article

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Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition (English)

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object named as

Els F Halff

2

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John D. Lambris

object named as

John D Lambris

3

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author name string

Bert J C Janssen

1

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Piet Gros

4

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language of work or name

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publication date

5 October 2007

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Journal of Biological Chemistry

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282

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40

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29241-7

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Complement. First of two parts

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Solution structure of Compstatin, a potent complement inhibitor

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The structural basis of compstatin activity examined by structure-function-based design of peptide analogs and NMR.

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C3 activation is inhibited by analogs of compstatin but not by serine protease inhibitors or peptidyl alpha-ketoheterocycles

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Binding kinetics, structure-activity relationship, and biotransformation of the complement inhibitor compstatin

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Thermodynamic studies on the interaction of the third complement component and its inhibitor, compstatin

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Design and NMR characterization of active analogues of compstatin containing non-natural amino acids

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Compstatin inhibits complement activation by binding to the beta-chain of complement factor 3.

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Structures of complement component C3 provide insights into the function and evolution of immunity

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Structure of C3b reveals conformational changes that underlie complement activity

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The structure of bovine complement component 3 reveals the basis for thioester function

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Structure of C3b in complex with CRIg gives insights into regulation of complement activation

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Structural transitions of complement component C3 and its activation products

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Isolation of a fragment (C3a) of the third component of human complement containing anaphylatoxin and chemotactic activity and description of an anaphylatoxin inactivator of human serum

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The CCP4 suite: programs for protein crystallography

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Use of non-crystallographic symmetry in protein structure refinement

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Compstatin, a peptide inhibitor of complement, exhibits species-specific binding to complement component C3.

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Structural insights into the central complement component C3.

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A structural basis for complement inhibition by Staphylococcus aureus

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Improvement of the anti-C3 activity of compstatin using rational and combinatorial approaches

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Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase

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Compstatin, a peptide inhibitor of C3, prolongs survival of ex vivo perfused pig xenografts

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Inhibition of Heparin/Protamine Complex-Induced Complement Activation by Compstatin in Baboons

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Hydrophobic Effect and Hydrogen Bonds Account for the Improved Activity of a Complement Inhibitor, Compstatin

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