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| - | [[Image:1tn8.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1tn8| PDB=1tn8 | SCENE= }} | | {{STRUCTURE_1tn8| PDB=1tn8 | SCENE= }} |
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| - | '''Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution'''
| + | ===Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution=== |
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| - | ==Overview==
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| - | Post-translational modifications are essential for the proper function of many proteins in the cell. The attachment of an isoprenoid lipid (a process termed prenylation) by protein farnesyltransferase (FTase) or geranylgeranyltransferase type I (GGTase-I) is essential for the function of many signal transduction proteins involved in growth, differentiation, and oncogenesis. FTase and GGTase-I (also called the CaaX prenyltransferases) recognize protein substrates with a C-terminal tetrapeptide recognition motif called the Ca1a2X box. These enzymes possess distinct but overlapping protein substrate specificity that is determined primarily by the sequence identity of the Ca1a2X motif. To determine how the identity of the Ca1a2X motif residues and sequence upstream of this motif affect substrate binding, we have solved crystal structures of FTase and GGTase-I complexed with a total of eight cognate and cross-reactive substrate peptides, including those derived from the C termini of the oncoproteins K-Ras4B, H-Ras and TC21. These structures suggest that all peptide substrates adopt a common binding mode in the FTase and GGTase-I active site. Unexpectedly, while the X residue of the Ca1a2X motif binds in the same location for all GGTase-I substrates, the X residue of FTase substrates can bind in one of two different sites. Together, these structures outline a series of rules that govern substrate peptide selectivity; these rules were utilized to classify known protein substrates of CaaX prenyltransferases and to generate a list of hypothetical substrates within the human genome.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15451670}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15451670 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15451670}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ra]] | | [[Category: Ra]] |
| | [[Category: Substrate selectivity]] | | [[Category: Substrate selectivity]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:09:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:04:42 2008'' |
Revision as of 20:04, 28 July 2008
Template:STRUCTURE 1tn8
Protein Farnesyltransferase Complexed with a H-Ras Peptide Substrate and a FPP Analog at 2.25A Resolution
Template:ABSTRACT PUBMED 15451670
About this Structure
1TN8 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity., Reid TS, Terry KL, Casey PJ, Beese LS, J Mol Biol. 2004 Oct 15;343(2):417-33. PMID:15451670
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