Literature DB >> 12520056

MolMovDB: analysis and visualization of conformational change and structural flexibility.

Nathaniel Echols1, Duncan Milburn, Mark Gerstein.   

Abstract

The Database of Macromolecular Movements (http://MolMovDB.org) is a collection of data and software pertaining to flexibility in protein and RNA structures. The database is organized into two parts. Firstly, a collection of 'morphs' of solved structures representing different states of a molecule provides quantitative data for flexibility and a number of graphical representations. Secondly, a classification of known motions according to type of conformational change (e.g. 'hinged domain' or 'allosteric') incorporates textual annotation and information from the literature relating to the motion, linking together many of the morphs. A variety of subsets of the morphs are being developed for use in statistical analyses. In particular, for each subset it is possible to derive distributions of various motional quantities (e.g. maximum rotation) that can be used to place a specific motion in context as being typical or atypical for a given population. Over the past year, the database has been greatly expanded and enhanced to incorporate new structures and to improve the quality of data. The 'morph server', which enables users of the database to add new morphs either from their own research or the PDB, has also been enhanced to handle nucleic acid structures and multi-chain complexes.

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Year:  2003        PMID: 12520056      PMCID: PMC165551          DOI: 10.1093/nar/gkg104

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


  11 in total

1.  The Protein Data Bank.

Authors:  H M Berman; J Westbrook; Z Feng; G Gilliland; T N Bhat; H Weissig; I N Shindyalov; P E Bourne
Journal:  Nucleic Acids Res       Date:  2000-01-01       Impact factor: 16.971

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.  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

4.  Structure of the 30S ribosomal subunit.

Authors:  B T Wimberly; D E Brodersen; W M Clemons; R J Morgan-Warren; A P Carter; C Vonrhein; T Hartsch; V Ramakrishnan
Journal:  Nature       Date:  2000-09-21       Impact factor: 49.962

5.  Normal mode analysis of macromolecular motions in a database framework: developing mode concentration as a useful classifying statistic.

Authors:  W G Krebs; Vadim Alexandrov; Cyrus A Wilson; Nathaniel Echols; Haiyuan Yu; Mark Gerstein
Journal:  Proteins       Date:  2002-09-01

6.  Crystallography & NMR system: A new software suite for macromolecular structure determination.

Authors:  A T Brünger; P D Adams; G M Clore; W L DeLano; P Gros; R W Grosse-Kunstleve; J S Jiang; J Kuszewski; M Nilges; N S Pannu; R J Read; L M Rice; T Simonson; G L Warren
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1998-09-01

7.  A database of macromolecular motions.

Authors:  M Gerstein; W Krebs
Journal:  Nucleic Acids Res       Date:  1998-09-15       Impact factor: 16.971

8.  CATH--a hierarchic classification of protein domain structures.

Authors:  C A Orengo; A D Michie; S Jones; D T Jones; M B Swindells; J M Thornton
Journal:  Structure       Date:  1997-08-15       Impact factor: 5.006

9.  SCOP: a structural classification of proteins database for the investigation of sequences and structures.

Authors:  A G Murzin; S E Brenner; T Hubbard; C Chothia
Journal:  J Mol Biol       Date:  1995-04-07       Impact factor: 5.469

Review 10.  Structural mechanisms for domain movements in proteins.

Authors:  M Gerstein; A M Lesk; C Chothia
Journal:  Biochemistry       Date:  1994-06-07       Impact factor: 3.162

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  65 in total

1.  Transconformations of the SERCA1 Ca-ATPase: a normal mode study.

Authors:  Nathalie Reuter; Konrad Hinsen; Jean-Jacques Lacapère
Journal:  Biophys J       Date:  2003-10       Impact factor: 4.033

2.  Information Visualization Techniques in Bioinformatics during the Postgenomic Era.

Authors:  Ying Tao; Yang Liu; Carol Friedman; Yves A Lussier
Journal:  Drug Discov Today Biosilico       Date:  2004-11

3.  Molecular basis of BACH1/FANCJ recognition by TopBP1 in DNA replication checkpoint control.

Authors:  Charles Chung Yun Leung; Zihua Gong; Junjie Chen; J N Mark Glover
Journal:  J Biol Chem       Date:  2010-12-02       Impact factor: 5.157

4.  Normal modes for predicting protein motions: a comprehensive database assessment and associated Web tool.

Authors:  Vadim Alexandrov; Ursula Lehnert; Nathaniel Echols; Duncan Milburn; Donald Engelman; Mark Gerstein
Journal:  Protein Sci       Date:  2005-03       Impact factor: 6.725

5.  iGNM: a database of protein functional motions based on Gaussian Network Model.

Authors:  Lee-Wei Yang; Xiong Liu; Christopher J Jursa; Mark Holliman; A J Rader; Hassan A Karimi; Ivet Bahar
Journal:  Bioinformatics       Date:  2005-04-28       Impact factor: 6.937

Review 6.  Coarse-grained normal mode analysis in structural biology.

Authors:  Ivet Bahar; A J Rader
Journal:  Curr Opin Struct Biol       Date:  2005-10       Impact factor: 6.809

7.  Structure-based engineering of internal cavities in coiled-coil peptides.

Authors:  Maneesh K Yadav; James E Redman; Luke J Leman; Julietta M Alvarez-Gutiérrez; Yanming Zhang; C David Stout; M Reza Ghadiri
Journal:  Biochemistry       Date:  2005-07-19       Impact factor: 3.162

8.  Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures.

Authors:  Kelly L Damm; Heather A Carlson
Journal:  Biophys J       Date:  2006-03-24       Impact factor: 4.033

9.  A method for finding candidate conformations for molecular replacement using relative rotation between domains of a known structure.

Authors:  Jay I Jeong; Eaton E Lattman; Gregory S Chirikjian
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2006-03-18

10.  How environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation.

Authors:  Hyunbum Jang; Paul S Crozier; Mark J Stevens; Thomas B Woolf
Journal:  Biophys J       Date:  2004-07       Impact factor: 4.033

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