5p21
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| 5p21, resolution 1.35Å () | |||||||||
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| Ligands: | , | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSISREFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS
Template:ABSTRACT PUBMED 2196171
About this StructureAbout this Structure
5p21 is a 1 chain structure with sequence from Homo sapiens. The April 2012 RCSB PDB Molecule of the Month feature on Ras Protein by David Goodsell is 10.2210/rcsb_pdb/mom_2012_4. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
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- ↑ Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 1990 Aug;9(8):2351-9. PMID:2196171
- ↑ Ho YS, Swenson L, Derewenda U, Serre L, Wei Y, Dauter Z, Hattori M, Adachi T, Aoki J, Arai H, Inoue K, Derewenda ZS. Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer. Nature. 1997 Jan 2;385(6611):89-93. PMID:8985254 doi:10.1038/385089a0
- ↑ Ma J, Karplus M. Ligand-induced conformational changes in ras p21: a normal mode and energy minimization analysis. J Mol Biol. 1997 Nov 21;274(1):114-31. PMID:9398520 doi:10.1006/jmbi.1997.1313
- ↑ Hayward S. Peptide-plane flipping in proteins. Protein Sci. 2001 Nov;10(11):2219-27. PMID:11604529 doi:10.1110/ps.23101
- ↑ Carta C, Pantaleoni F, Bocchinfuso G, Stella L, Vasta I, Sarkozy A, Digilio C, Palleschi A, Pizzuti A, Grammatico P, Zampino G, Dallapiccola B, Gelb BD, Tartaglia M. Germline missense mutations affecting KRAS Isoform B are associated with a severe Noonan syndrome phenotype. Am J Hum Genet. 2006 Jul;79(1):129-35. Epub 2006 May 1. PMID:16773572 doi:10.1086/504394