1pht
From Proteopedia
(New page: 200px<br /> <applet load="1pht" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pht, resolution 2.0Å" /> '''PHOSPHATIDYLINOSITOL...) |
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caption="1pht, resolution 2.0Å" /> | caption="1pht, resolution 2.0Å" /> | ||
'''PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN, RESIDUES 1-85'''<br /> | '''PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN, RESIDUES 1-85'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PHT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1PHT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PHT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:40:05 2008'' |
Revision as of 14:40, 15 February 2008
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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
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