PMID- 10338209
OWN - NLM
STAT- MEDLINE
DCOM- 19990615
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 97
IP  - 4
DP  - 1999 May 14
TI  - Crystal structure of the tandem phosphatase domains of RPTP LAR.
PG  - 449-57
AB  - Most receptor-like protein tyrosine phosphatases (RPTPs) contain two conserved
      phosphatase domains (D1 and D2) in their intracellular region. The
      carboxy-terminal D2 domain has little or no catalytic activity. The crystal
      structure of the tandem D1 and D2 domains of the human RPTP LAR revealed that the
      tertiary structures of the LAR D1 and D2 domains are very similar to each other, 
      with the exception of conformational differences at two amino acid positions in
      the D2 domain. Site-directed mutational changes at these positions
      (Leu-1644-to-Tyr and Glu-1779-to-Asp) conferred a robust PTPase activity to the
      D2 domain. The catalytic sites of both domains are accessible, in contrast to the
      dimeric blocked orientation model previously suggested. The relative orientation 
      of the LAR D1 and D2 domains, constrained by a short linker, is stabilized by
      extensive interdomain interactions, suggesting that this orientation might be
      favored in solution.
FAU - Nam, H J
AU  - Nam HJ
AD  - Dana-Farber Cancer Institute and Department of Biological Chemistry and Molecular
      Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
FAU - Poy, F
AU  - Poy F
FAU - Krueger, N X
AU  - Krueger NX
FAU - Saito, H
AU  - Saito H
FAU - Frederick, C A
AU  - Frederick CA
LA  - eng
SI  - PDB/1LAR
GR  - GM 53415/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Receptors, Cell Surface)
RN  - EC 3.1.3.48 (PTPRA protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 4)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Crystallography, X-Ray
MH  - Humans
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutagenesis
MH  - *Protein Conformation
MH  - Protein Tyrosine Phosphatases/*chemistry/genetics/metabolism
MH  - Receptor-Like Protein Tyrosine Phosphatases, Class 4
MH  - *Receptors, Cell Surface
MH  - Sequence Homology, Amino Acid
EDAT- 1999/05/25 00:00
MHDA- 1999/05/25 00:01
CRDT- 1999/05/25 00:00
PHST- 1999/05/25 00:00 [pubmed]
PHST- 1999/05/25 00:01 [medline]
PHST- 1999/05/25 00:00 [entrez]
AID - S0092-8674(00)80755-2 [pii]
AID - 10.1016/s0092-8674(00)80755-2 [doi]
PST - ppublish
SO  - Cell. 1999 May 14;97(4):449-57. doi: 10.1016/s0092-8674(00)80755-2.