Literature DB >> 10611401

Exploring the conformational diversity of loops on conserved frameworks.

W Li1, S Liang, R Wang, L Lai, Y Han.   

Abstract

Loops are structurally variable regions, but the secondary structural elements bracing loops are often conserved. Motifs with similar secondary structures exist in the same and different protein families. In this study, we made an all-PDB-based analysis and produced 495 motif families accessible from the Internet. Every motif family contains some variable loops spanning a common framework (a pair of secondary structures). The diversity of loops and the convergence of frameworks were examined. In addition, we also identified 119 loops with conformational changes in different PDB files. These materials can give some directions for functional loop design and flexible docking.

Mesh:

Substances:

Year:  1999        PMID: 10611401     DOI: 10.1093/protein/12.12.1075

Source DB:  PubMed          Journal:  Protein Eng        ISSN: 0269-2139


  3 in total

1.  Structure modeling of the chemokine receptor CCR5: implications for ligand binding and selectivity.

Authors:  M Germana Paterlini
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

2.  Outliers in SAR and QSAR: 2. Is a flexible binding site a possible source of outliers?

Authors:  Ki Hwan Kim
Journal:  J Comput Aided Mol Des       Date:  2007-07-24       Impact factor: 3.686

3.  Mining protein loops using a structural alphabet and statistical exceptionality.

Authors:  Leslie Regad; Juliette Martin; Gregory Nuel; Anne-Claude Camproux
Journal:  BMC Bioinformatics       Date:  2010-02-04       Impact factor: 3.169

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.