1fpr: Difference between revisions
New page: left|200px<br /> <applet load="1fpr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fpr, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1fpr. | [[Image:1fpr.jpg|left|200px]]<br /><applet load="1fpr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1fpr" size=" | |||
caption="1fpr, resolution 2.5Å" /> | caption="1fpr, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.'''<br /> | '''CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
1FPR 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:// | 1FPR 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=1FPR OCA]. | ||
==Reference== | ==Reference== | ||
| Line 24: | Line 23: | ||
[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:48:42 2008'' | ||
Revision as of 16:48, 15 February 2008
|
CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN THE CATALYTIC DOMAIN OF SHP-1 AND AN IN VITRO PEPTIDE SUBSTRATE PY469 DERIVED FROM SHPS-1.
OverviewOverview
The substrate specificity of the catalytic domain of SHP-1, an important, regulator in the proliferation and development of hematopoietic cells, is, critical for understanding the physiological functions of SHP-1. Here we, report the crystal structures of the catalytic domain of SHP-1 complexed, with two peptide substrates derived from SIRPalpha, a member of the, signal-regulatory proteins. We show that the variable beta5-loop-beta6, motif confers SHP-1 substrate specificity at the P-4 and further, N-terminal subpockets. We also observe a novel residue shift at P-2, the, highly conserved subpocket in protein- tyrosine phosphatases. Our, observations provide new insight into the substrate specificity of SHP-1.
About this StructureAbout this Structure
1FPR 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
Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1., Yang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW, J Biol Chem. 2000 Feb 11;275(6):4066-71. PMID:10660565
Page seeded by OCA on Fri Feb 15 15:48:42 2008