Literature DB >> 8325386

Movable lobes and flexible loops in proteins. Structural deformations that control biochemical activity.

E S Kempner1.   

Abstract

Two classes of protein whose structure is modified by small ligands are reviewed. Proteins of one group contain two massive domains joined by a flexible link; in response to small molecules, the two lobes approach and enclose the ligand. In the other, a short segment of amino acids moves as a flexible loop over the ligand which often is trapped in a non-aqueous environment. Biochemical reaction rates are altered dramatically by these movements.

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Year:  1993        PMID: 8325386     DOI: 10.1016/0014-5793(93)81749-p

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  21 in total

Review 1.  The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors.

Authors:  C B Felder; R C Graul; A Y Lee; H P Merkle; W Sadee
Journal:  AAPS PharmSci       Date:  1999

2.  Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site.

Authors:  Ingo P Korndörfer; Arne Skerra
Journal:  Protein Sci       Date:  2002-04       Impact factor: 6.725

3.  Evolution of tRNA nucleotidyltransferases: a small deletion generated CC-adding enzymes.

Authors:  Anne Neuenfeldt; Andrea Just; Heike Betat; Mario Mörl
Journal:  Proc Natl Acad Sci U S A       Date:  2008-06-03       Impact factor: 11.205

4.  Fluorescamine Labeling for Assessment of Protein Conformational Change and Binding Affinity in Protein-Nanoparticle Interaction.

Authors:  Yaokai Duan; Yang Liu; Wen Shen; Wenwan Zhong
Journal:  Anal Chem       Date:  2017-11-08       Impact factor: 6.986

5.  Determination of the amino acid requirements for a protein hinge in triosephosphate isomerase.

Authors:  J Sun; N S Sampson
Journal:  Protein Sci       Date:  1998-07       Impact factor: 6.725

6.  Molecular dynamics simulations of protein-tyrosine phosphatase 1B. I. ligand-induced changes in the protein motions.

Authors:  G H Peters; T M Frimurer; J N Andersen; O H Olsen
Journal:  Biophys J       Date:  1999-07       Impact factor: 4.033

7.  Function of a conserved sequence motif in biotin holoenzyme synthetases.

Authors:  K Kwon; D Beckett
Journal:  Protein Sci       Date:  2000-08       Impact factor: 6.725

8.  Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120.

Authors:  A Chilkoti; P H Tan; P S Stayton
Journal:  Proc Natl Acad Sci U S A       Date:  1995-02-28       Impact factor: 11.205

9.  Hydrogen bond residue positioning in the 599-611 loop of thimet oligopeptidase is required for substrate selection.

Authors:  Lisa A Bruce; Jeffrey A Sigman; Danica Randall; Scott Rodriguez; Michelle M Song; Yi Dai; Donald E Elmore; Amanda Pabon; Marc J Glucksman; Adele J Wolfson
Journal:  FEBS J       Date:  2008-11       Impact factor: 5.542

10.  On the role of protein structural dynamics in the catalytic activity and thermostability of serine protease subtilisin Carlsberg.

Authors:  Miraida Pagán; Ricardo J Solá; Kai Griebenow
Journal:  Biotechnol Bioeng       Date:  2009-05-01       Impact factor: 4.530

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