Literature DB >> 1603812

Common features of the conformations of antigen-binding loops in immunoglobulins and application to modeling loop conformations.

A Tramontano1, A M Lesk.   

Abstract

Using database screening techniques we have examined the relationship between antigen-binding loops in immunoglobulins, and regions of similar conformation in other protein families. The conformations of most antigen-binding loops are not unique to immunoglobulins. But in many cases, the geometrical relationship between the loop and the peptides flanking it differs between the immunoglobulins and other structures with the same loop. We assess model building by data base screening, compared with that based on canonical structures.

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Year:  1992        PMID: 1603812     DOI: 10.1002/prot.340130306

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  19 in total

1.  Modeling of loops in protein structures.

Authors:  A Fiser; R K Do; A Sali
Journal:  Protein Sci       Date:  2000-09       Impact factor: 6.725

2.  Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction.

Authors:  Zhexin Xiang; Cinque S Soto; Barry Honig
Journal:  Proc Natl Acad Sci U S A       Date:  2002-05-28       Impact factor: 11.205

3.  A fold-recognition approach to loop modeling.

Authors:  Christer Levefelt; Dan Lundh
Journal:  J Mol Model       Date:  2005-11-08       Impact factor: 1.810

4.  Structural models of antibody variable fragments: a method for investigating binding mechanisms.

Authors:  S Petit; F Brard; G Coquerel; G Perez; F Tron
Journal:  J Comput Aided Mol Des       Date:  1998-03       Impact factor: 3.686

5.  Does conformational free energy distinguish loop conformations in proteins?

Authors:  J L Pellequer; S W Chen
Journal:  Biophys J       Date:  1997-11       Impact factor: 4.033

6.  Linkers of secondary structures in proteins.

Authors:  V Geetha; P J Munson
Journal:  Protein Sci       Date:  1997-12       Impact factor: 6.725

7.  Mutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome c.

Authors:  J S Fetrow; U Dreher; D J Wiland; D L Schaak; T L Boose
Journal:  Protein Sci       Date:  1998-04       Impact factor: 6.725

8.  Molecular and structural analysis of nuclear localizing anti-DNA lupus antibodies.

Authors:  M H Foster; T Kieber-Emmons; M Ohliger; M P Madaio
Journal:  Immunol Res       Date:  1994       Impact factor: 2.829

9.  Structural predictions of the binding site architecture for monoclonal antibody NC6.8 using computer-aided molecular modeling, ligand binding, and spectroscopy.

Authors:  M Viswanathan; J M Anchin; P R Droupadi; C Mandal; D S Linthicum; S Subramaniam
Journal:  Biophys J       Date:  1995-09       Impact factor: 4.033

10.  Cloning, characterization, and modeling of a monoclonal anti-human transferrin antibody that competes with the transferrin receptor.

Authors:  M Orlandini; A Santucci; A Tramontano; P Neri; S Oliviero
Journal:  Protein Sci       Date:  1994-09       Impact factor: 6.725

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