Literature DB >> 9722650

A database of macromolecular motions.

M Gerstein1, W Krebs.   

Abstract

We describe a database of macromolecular motions meant to be of general use to the structural community. The database, which is accessible on the World Wide Web with an entry point at http://bioinfo.mbb.yale.edu/MolMovDB , attempts to systematize all instances of protein and nucleic acid movement for which there is at least some structural information. At present it contains >120 motions, most of which are of proteins. Protein motions are further classified hierarchically into a limited number of categories, first on the basis of size (distinguishing between fragment, domain and subunit motions) and then on the basis of packing. Our packing classification divides motions into various categories (shear, hinge, other) depending on whether or not they involve sliding over a continuously maintained and tightly packed interface. In addition, the database provides some indication about the evidence behind each motion (i.e. the type of experimental information or whether the motion is inferred based on structural similarity) and attempts to describe many aspects of a motion in terms of a standardized nomenclature (e.g. the maximum rotation, the residue selection of a fixed core, etc.). Currently, we use a standard relational design to implement the database. However, the complexity and heterogeneity of the information kept in the database makes it an ideal application for an object-relational approach, and we are moving it in this direction. Specifically, in terms of storing complex information, the database contains plausible representations for motion pathways, derived from restrained 3D interpolation between known endpoint conformations. These pathways can be viewed in a variety of movie formats, and the database is associated with a server that can automatically generate these movies from submitted coordinates.

Mesh:

Substances:

Year:  1998        PMID: 9722650      PMCID: PMC147832          DOI: 10.1093/nar/26.18.4280

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  93 in total

Review 1.  Structure-based strategies for drug design and discovery.

Authors:  I D Kuntz
Journal:  Science       Date:  1992-08-21       Impact factor: 47.728

2.  The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage.

Authors:  W G Scott; J T Finch; A Klug
Journal:  Cell       Date:  1995-06-30       Impact factor: 41.582

Review 3.  The prion folding problem.

Authors:  P M Harrison; P Bamborough; V Daggett; S B Prusiner; F E Cohen
Journal:  Curr Opin Struct Biol       Date:  1997-02       Impact factor: 6.809

Review 4.  Glycogen phosphorylase. The structural basis of the allosteric response and comparison with other allosteric proteins.

Authors:  L N Johnson; D Barford
Journal:  J Biol Chem       Date:  1990-02-15       Impact factor: 5.157

Review 5.  Protein folding: the endgame.

Authors:  M Levitt; M Gerstein; E Huang; S Subbiah; J Tsai
Journal:  Annu Rev Biochem       Date:  1997       Impact factor: 23.643

6.  Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes.

Authors:  J W Ponder; F M Richards
Journal:  J Mol Biol       Date:  1987-02-20       Impact factor: 5.469

Review 7.  Mechanisms of cooperativity and allosteric regulation in proteins.

Authors:  M F Perutz
Journal:  Q Rev Biophys       Date:  1989-05       Impact factor: 5.318

8.  Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers.

Authors:  M Gerstein; G Schulz; C Chothia
Journal:  J Mol Biol       Date:  1993-01-20       Impact factor: 5.469

9.  Glucose-induced conformational change in yeast hexokinase.

Authors:  W S Bennett; T A Steitz
Journal:  Proc Natl Acad Sci U S A       Date:  1978-10       Impact factor: 11.205

10.  Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible.

Authors:  D G Donne; J H Viles; D Groth; I Mehlhorn; T L James; F E Cohen; S B Prusiner; P E Wright; H J Dyson
Journal:  Proc Natl Acad Sci U S A       Date:  1997-12-09       Impact factor: 11.205

View more
  116 in total

1.  Predicting conformational switches in proteins.

Authors:  M Young; K Kirshenbaum; K A Dill; S Highsmith
Journal:  Protein Sci       Date:  1999-09       Impact factor: 6.725

2.  PartsList: a web-based system for dynamically ranking protein folds based on disparate attributes, including whole-genome expression and interaction information.

Authors:  J Qian; B Stenger; C A Wilson; J Lin; R Jansen; S A Teichmann; J Park; W G Krebs; H Yu; V Alexandrov; N Echols; M Gerstein
Journal:  Nucleic Acids Res       Date:  2001-04-15       Impact factor: 16.971

3.  Induced fit in arginine kinase.

Authors:  G Zhou; W R Ellington; M S Chapman
Journal:  Biophys J       Date:  2000-03       Impact factor: 4.033

4.  The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework.

Authors:  W G Krebs; M Gerstein
Journal:  Nucleic Acids Res       Date:  2000-04-15       Impact factor: 16.971

Review 5.  Folding and binding cascades: dynamic landscapes and population shifts.

Authors:  S Kumar; B Ma; C J Tsai; N Sinha; R Nussinov
Journal:  Protein Sci       Date:  2000-01       Impact factor: 6.725

6.  Point mutations and sequence variability in proteins: redistributions of preexisting populations.

Authors:  N Sinha; R Nussinov
Journal:  Proc Natl Acad Sci U S A       Date:  2001-03-13       Impact factor: 11.205

7.  Escherichia coli RNA polymerase core and holoenzyme structures.

Authors:  R D Finn; E V Orlova; B Gowen; M Buck; M van Heel
Journal:  EMBO J       Date:  2000-12-15       Impact factor: 11.598

Review 8.  Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations.

Authors:  Buyong Ma; Maxim Shatsky; Haim J Wolfson; Ruth Nussinov
Journal:  Protein Sci       Date:  2002-02       Impact factor: 6.725

9.  SPINE: an integrated tracking database and data mining approach for identifying feasible targets in high-throughput structural proteomics.

Authors:  P Bertone; Y Kluger; N Lan; D Zheng; D Christendat; A Yee; A M Edwards; C H Arrowsmith; G T Montelione; M Gerstein
Journal:  Nucleic Acids Res       Date:  2001-07-01       Impact factor: 16.971

10.  Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures.

Authors:  W Wriggers; R K Agrawal; D L Drew; A McCammon; J Frank
Journal:  Biophys J       Date:  2000-09       Impact factor: 4.033

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.