PMID- 10531064
OWN - NLM
STAT- MEDLINE
DCOM- 19991105
LR  - 20190619
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 286
IP  - 5440
DP  - 1999 Oct 22
TI  - Crystal structure of the ectodomain of human transferrin receptor.
PG  - 779-82
AB  - The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated
      endocytosis and reemergence at the cell surface, importing iron-loaded
      transferrin (Tf) and recycling apotransferrin after discharge of iron in the
      endosome. The crystal structure of the dimeric ectodomain of the human TfR,
      determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One 
      domain closely resembles carboxy- and aminopeptidases, and features of membrane
      glutamate carboxypeptidase can be deduced from the TfR structure. A model is
      proposed for Tf binding to the receptor.
FAU - Lawrence, C M
AU  - Lawrence CM
AD  - Howard Hughes Medical Institute and Children's Hospital Laboratory of Molecular
      Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.
FAU - Ray, S
AU  - Ray S
FAU - Babyonyshev, M
AU  - Babyonyshev M
FAU - Galluser, R
AU  - Galluser R
FAU - Borhani, D W
AU  - Borhani DW
FAU - Harrison, S C
AU  - Harrison SC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Ferric Compounds)
RN  - 0 (Receptors, Transferrin)
RN  - 0 (Transferrin)
RN  - EC 3.4.- (Carboxypeptidases)
RN  - EC 3.4.17.11 (glutamate carboxypeptidase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - CHO Cells
MH  - Carboxypeptidases/chemistry
MH  - Cell Membrane/chemistry
MH  - Conserved Sequence
MH  - Cricetinae
MH  - Crystallography, X-Ray
MH  - Dimerization
MH  - Ferric Compounds/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Receptors, Transferrin/*chemistry/metabolism
MH  - Transferrin/metabolism
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - 7905 [pii]
AID - 10.1126/science.286.5440.779 [doi]
PST - ppublish
SO  - Science. 1999 Oct 22;286(5440):779-82. doi: 10.1126/science.286.5440.779.