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821p

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[[Image:821p.gif|left|200px]]<br /><applet load="821p" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:821p.gif|left|200px]]
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caption="821p, resolution 1.5&Aring;" />
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'''THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLYCINE-12 MUTANT OF P21H-RAS'''<br />
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{{Structure
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|PDB= 821p |SIZE=350|CAPTION= <scene name='initialview01'>821p</scene>, resolution 1.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLYCINE-12 MUTANT OF P21H-RAS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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821P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=821P OCA].
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821P is a [[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=821P OCA].
==Reference==
==Reference==
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Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras., Franken SM, Scheidig AJ, Krengel U, Rensland H, Lautwein A, Geyer M, Scheffzek K, Goody RS, Kalbitzer HR, Pai EF, et al., Biochemistry. 1993 Aug 24;32(33):8411-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8357792 8357792]
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Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras., Franken SM, Scheidig AJ, Krengel U, Rensland H, Lautwein A, Geyer M, Scheffzek K, Goody RS, Kalbitzer HR, Pai EF, et al., Biochemistry. 1993 Aug 24;32(33):8411-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8357792 8357792]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oncogene protein]]
[[Category: oncogene protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:17:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:15:11 2008''

Revision as of 17:15, 20 March 2008

Image:821p.gif


PDB ID 821p

Drag the structure with the mouse to rotate
, resolution 1.5Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLYCINE-12 MUTANT OF P21H-RAS


Contents

Overview

The three-dimensional structures and biochemical properties of two mutants of the G-domain (residues 1-166) of p21H-ras, p21 (G12D) and p21 (G12P), have been determined in the triphosphate-bound form using guanosine 5'-(beta,gamma-imido)triphosphate (GppNHp). They correspond to the most frequent oncogenic and the only nononcogenic mutation of Gly-12, respectively. The G12D mutation is the only mutant analyzed so far that crystallizes in a space group different from wild type, and the atomic model of the protein shows the most drastic changes of structure around the active site as compared to wild-type p21. This is due to the interactions of the aspartic acid side chain with Tyr-32, Gln-61, and the gamma-phosphate, which result in reduced mobility of these structural elements. The interaction between the carboxylate group of Asp-12 and the gamma-phosphate is mediated by a shared proton, which we show by 31P NMR measurements to exist in solution as well. The structure of p21 (G12P) is remarkably similar to that of wild-type p21 in the active site, including the position of the nucleophilic water. The pyrrolidine ring of Pro-12 points outward and seems to be responsible for the weaker affinity toward GAP (GTPase-activating protein) and the failure of GAP to stimulate GTP hydrolysis.

Disease

Known diseases associated with this structure: Bladder cancer, somatic OMIM:[190020], Costello syndrome OMIM:[190020], Thyroid carcinoma, follicular, somatic OMIM:[190020]

About this Structure

821P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras., Franken SM, Scheidig AJ, Krengel U, Rensland H, Lautwein A, Geyer M, Scheffzek K, Goody RS, Kalbitzer HR, Pai EF, et al., Biochemistry. 1993 Aug 24;32(33):8411-20. PMID:8357792

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