Structure and thermal stability of the extracellular fragment of human transferrin receptor at extracellular and endosomal pH.


Abstract

Fourier transform infrared spectroscopy has been used to study the solution structure and thermal stability of the extracellular fragment of human transferrin receptor (tfRt) at extracellular and endosomal pH. At extracellular pH tfRt is composed of 56% alpha-helix, 19% beta-sheet and 14% turns. Upon acidification to endosomal pH the alpha-helical content of the protein is reduced and the beta-sheet content increased by nearly 10%. At extracellular pH, the midpoint temperature of thermal denaturation (Tm) for the loss of secondary and tertiary structure, and the formation of aggregated structures, is 71 degrees C. At endosomal pH this temperature is reduced by approximately 15 degrees C. The apparent entropies of thermal denaturation indicate that the native structure of tfRt at endosomal pH is far more flexible than at extracellular pH. Study holds ProTherm entries: 10391, 10392 Extra Details: fourier transform infrared spectroscopy; secondary structure;,tertiary structure; thermal stability; pH-dependent conformational change

Submission Details

ID: CZmnu9RG3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details
Hadden JM;Bloemendal M;Haris PI;van Stokkum IH;Chapman D;Srai SK,FEBS Lett. (1994) Structure and thermal stability of the extracellular fragment of human transferrin receptor at extracellular and endosomal pH. PMID:7915240
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
3KAS 2010-03-09 2.4 Machupo virus GP1 bound to human transferrin receptor 1
1DE4 2000-01-19 2.8 HEMOCHROMATOSIS PROTEIN HFE COMPLEXED WITH TRANSFERRIN RECEPTOR
2NSU 2007-03-27 27.0 Crystal structure of the ectodomain of human transferrin receptor fitted into a cryo-EM reconstruction of canine parvovirus and feline transferrin receptor complex
1CX8 1999-09-09 3.2 CRYSTAL STRUCTURE OF THE ECTODOMAIN OF HUMAN TRANSFERRIN RECEPTOR
3S9L 2011-08-10 3.22 Complex between transferrin receptor 1 and transferrin with iron in the N-Lobe, cryocooled 2
3S9N 2011-08-10 3.25 Complex between transferrin receptor 1 and transferrin with iron in the N-Lobe, room temperature
3S9M 2011-08-10 3.32 Complex between transferrin receptor 1 and transferrin with iron in the N-Lobe, cryocooled 1
6D03 2018-06-20 3.68 Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; one molecule of parasite ligand.
6D04 2018-06-20 3.74 Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; two molecules of parasite ligand, subclass 1.
6D05 2018-06-20 3.8 Cryo-EM structure of a Plasmodium vivax invasion complex essential for entry into human reticulocytes; two molecules of parasite ligand, subclass 2.
6H5I 2019-03-27 3.9 Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex.
6GSR 2019-03-27 5.5 Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex at 5.5 Angstrom resolution.
1SUV 2004-04-13 7.5 Structure of Human Transferrin Receptor-Transferrin Complex

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
98.3 Transferrin receptor protein 1 Q5RDH6 TFR1_PONAB
100.0 Transferrin receptor protein 1 P02786 TFR1_HUMAN