(1)H, (15)N and (13)C resonance assignments of the two TPR domains from the human RPAP3 protein

Marie-Eve Chagot; Clémence Jacquemin; Christiane Branlant; Bruno Charpentier; Xavier Manival; Marc Quinternet

doi:10.1007/s12104-014-9552-4

(1)H, (15)N and (13)C resonance assignments of the two TPR domains from the human RPAP3 protein

Biomol NMR Assign. 2015 Apr;9(1):99-102. doi: 10.1007/s12104-014-9552-4. Epub 2014 Mar 26.

Authors

Marie-Eve Chagot¹, Clémence Jacquemin, Christiane Branlant, Bruno Charpentier, Xavier Manival, Marc Quinternet

Affiliation

¹ Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), UMR 7365 CNRS Université de Lorraine, Biopôle de l'Université de Lorraine, Campus Biologie Santé, 9 avenue de la forêt de Haye, CS 50184, 54505, Vandœuvre-lès-Nancy, France.

PMID: 24668569
DOI: 10.1007/s12104-014-9552-4

Abstract

We report the nearly complete (1)H, (15)N and (13)C resonance assignments of the two tetratricopeptide-repeat domains of the human RPAP3 protein, a co-chaperone of the heat-shock protein family.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Apoptosis Regulatory Proteins
Carrier Proteins / chemistry*
Humans
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular*
Protein Structure, Tertiary

Substances

Apoptosis Regulatory Proteins
Carrier Proteins
RPAP3 protein, human