1eag: Difference between revisions
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Revision as of 16:04, 30 October 2007
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SECRETED ASPARTIC PROTEINASE (SAP2) FROM CANDIDA ALBICANS COMPLEXED WITH A70450
OverviewOverview
BACKGROUND: Infections caused by Candida albicans, a common fungal, pathogen of humans, are increasing in incidence, necessitating development, of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is, considered an important virulence factor in these infections and might, offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C., albicans strains. RESULTS: The three-dimensional structures of SAP2, complexed with the tight-binding inhibitor A70450 (a synthetic hexapeptide, analogue) and with the general aspartic proteinase inhibitor pepstatin A, (a microbial natural product) have been determined to 2.1 A and 3.0 A, resolution, respectively. Although the protein structure retains the main, ... [(full description)]
About this StructureAbout this Structure
1EAG is a [Single protein] structure of sequence from [Candida albicans] with ODS and VAS as [ligands]. Active as [Candidapepsin], with EC number [3.4.23.24]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors., Cutfield SM, Dodson EJ, Anderson BF, Moody PC, Marshall CJ, Sullivan PA, Cutfield JF, Structure. 1995 Nov 15;3(11):1261-71. PMID:8591036
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