1pht
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1pht.jpg|left|200px]] | [[Image:1pht.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1pht", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1pht| PDB=1pht | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN, RESIDUES 1-85''' | '''PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN, RESIDUES 1-85''' | ||
| Line 29: | Line 26: | ||
[[Category: Liang, J.]] | [[Category: Liang, J.]] | ||
[[Category: Schreiber, S L.]] | [[Category: Schreiber, S L.]] | ||
| - | [[Category: | + | [[Category: P85-alpha subunit]] |
| - | [[Category: | + | [[Category: Phosphatidylinositol 3-kinase]] |
| - | [[Category: | + | [[Category: Sh3 domain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:06:06 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:06, 3 May 2008
PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN, RESIDUES 1-85
Overview
The P13K SH3 domain, residues 1 to 85 of the P1-3 kinase p85 subunit, has been characterized by X-ray diffraction. Crystals belonging to space group P4(3)2(1)2 diffract to 2.0 angstroms resolution and the structure was phased by single isomorphous replacement and anomalous scattering (SIRAS). As expected, the domain is a compact beta barrel with an over-all confirmation very similar to the independently determined NMR structures. The X-ray structure illuminates a discrepancy between the two NMR structures on the conformation of the loop region unique to P13K SH3. Furthermore, the ligand binding pockets of P13K SH3 domain are occupied by amino acid residues from symmetry-related P13K SH3 molecules: the C-terminal residues I(82) SPP of one and R18 of another. The interaction modes clearly resemble those observed for the P13K SH3 domain complexed with the synthetic peptide RLP1, a class 1 ligand, although there are significant differences. The solid-state interactions suggest a model of protein-protein aggregation that could be mediated by SH3 domains.
About this Structure
1PHT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of P13K SH3 domain at 20 angstroms resolution., Liang J, Chen JK, Schreiber ST, Clardy J, J Mol Biol. 1996 Apr 5;257(3):632-43. PMID:8648629 Page seeded by OCA on Sat May 3 05:06:06 2008
