1lar: Difference between revisions
New page: left|200px<br /> <applet load="1lar" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lar, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1lar.gif|left|200px]]<br /> | [[Image:1lar.gif|left|200px]]<br /><applet load="1lar" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1lar" size=" | |||
caption="1lar, resolution 2.0Å" /> | caption="1lar, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR'''<br /> | '''CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR'''<br /> | ||
==Overview== | ==Overview== | ||
Most receptor-like protein tyrosine phosphatases (RPTPs) contain two | 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. | ||
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
1LAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http:// | 1LAR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAR OCA]. | ||
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Frederick, C | [[Category: Frederick, C A.]] | ||
[[Category: Krueger, N.]] | [[Category: Krueger, N.]] | ||
[[Category: Nam, H | [[Category: Nam, H J.]] | ||
[[Category: Poy, F.]] | [[Category: Poy, F.]] | ||
[[Category: Saito, H.]] | [[Category: Saito, H.]] | ||
| Line 26: | Line 25: | ||
[[Category: tyrosine phosphatease]] | [[Category: tyrosine phosphatease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:11 2008'' | ||
Revision as of 14:43, 21 February 2008
|
CRYSTAL STRUCTURE OF THE TANDEM PHOSPHATASE DOMAINS OF RPTP LAR
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Leukemia, acute myeloid OMIM:[604763]
About this StructureAbout this Structure
1LAR is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the tandem phosphatase domains of RPTP LAR., Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA, Cell. 1999 May 14;97(4):449-57. PMID:10338209
Page seeded by OCA on Thu Feb 21 13:43:11 2008