Literature DB >> 19453194

Atomic-level mapping of antibody epitopes on a GPCR.

Cheryl Paes1, Jada Ingalls, Karan Kampani, Chidananda Sulli, Esha Kakkar, Meredith Murray, Valery Kotelnikov, Tiffani A Greene, Joseph B Rucker, Benjamin J Doranz.   

Abstract

Epitopes that define the immunodominant regions of conformationally complex integral membrane proteins have been difficult to reliably delineate. Here, a high-throughput approach termed shotgun mutagenesis was used to map the binding epitopes of five different monoclonal antibodies targeting the GPCR CCR5. The amino acids, and in some cases the atoms, that comprise the critical contact points of each epitope were identified, defining the immunodominant structures of this GPCR and their physicochemistry.

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Year:  2009        PMID： 19453194      PMCID： PMC2943208          DOI： 10.1021/ja900186n

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


  15 in total

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Journal:  J Biol Chem       Date:  1999-04-02       Impact factor: 5.157

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Review 4.  Anatomy of hot spots in protein interfaces.

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Review 7.  Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease.

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8.  Extracellular cysteines of CCR5 are required for chemokine binding, but dispensable for HIV-1 coreceptor activity.

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Journal:  J Biol Chem       Date:  1999-07-02       Impact factor: 5.157

9.  Differential inhibition of human immunodeficiency virus type 1 fusion, gp120 binding, and CC-chemokine activity by monoclonal antibodies to CCR5.

Authors:  W C Olson; G E Rabut; K A Nagashima; D N Tran; D J Anselma; S P Monard; J P Segal; D A Thompson; F Kajumo; Y Guo; J P Moore; P J Maddon; T Dragic
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  34 in total

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9.  High-Throughput Protein Engineering Improves the Antigenicity and Stability of Soluble HIV-1 Envelope Glycoprotein SOSIP Trimers.

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