1d8d: Difference between revisions
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[[Image:1d8d.png|left|200px]] | [[Image:1d8d.png|left|200px]] | ||
{{STRUCTURE_1d8d| PDB=1d8d | SCENE= }} | {{STRUCTURE_1d8d| PDB=1d8d | SCENE= }} | ||
===CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION=== | ===CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION=== | ||
{{ABSTRACT_PUBMED_10673434}} | {{ABSTRACT_PUBMED_10673434}} | ||
==About this Structure== | ==About this Structure== | ||
[[1d8d]] is a 3 chain structure of [[Farnesyltransferase]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8D OCA]. | |||
==See Also== | |||
*[[Farnesyltransferase|Farnesyltransferase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:010673434</ref><ref group="xtra">PMID:012374986</ref><references group="xtra"/> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Squalene synthase]] | [[Category: Squalene synthase]] | ||
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[[Category: Pftase]] | [[Category: Pftase]] | ||
[[Category: Ra]] | [[Category: Ra]] | ||
[[Category: Transferase]] | |||
Revision as of 12:00, 26 July 2012
CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION
Template:ABSTRACT PUBMED 10673434
About this Structure
1d8d is a 3 chain structure of Farnesyltransferase with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Long SB, Casey PJ, Beese LS. The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures. Structure. 2000 Feb 15;8(2):209-22. PMID:10673434
- Long SB, Casey PJ, Beese LS. Reaction path of protein farnesyltransferase at atomic resolution. Nature. 2002 Oct 10;419(6907):645-50. PMID:12374986 doi:10.1038/nature00986