1LAR

CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR

Summary for 1LAR

• Entry DOI: 10.2210/pdb1lar/pdb
• Descriptor: PROTEIN (LAR) (2 entities in total)
• Functional Keywords: tyrosine phosphatease, lar protein, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P10586
• Total number of polymer chains: 2
• Total formula weight: 132184.19

Authors

Nam, H.-J.,Poy, F.,Krueger, N.,Saito, H.,Frederick, C.A. (deposition date: 1999-04-20, release date: 2000-04-25, Last modification date: 2023-08-16)

Primary citation

Nam, H.J.,Poy, F.,Krueger, N.X.,Saito, H.,Frederick, C.A.
Crystal structure of the tandem phosphatase domains of RPTP LAR.
Cell(Cambridge,Mass.), 97:449-457, 1999

PubMed Abstract: 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.

PubMed: 10338209
DOI: 10.1016/S0092-8674(00)80755-2

Experimental method

X-RAY DIFFRACTION (2 Å)