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| - | [[Image:1eag.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1eag| PDB=1eag | SCENE= }} | | {{STRUCTURE_1eag| PDB=1eag | SCENE= }} |
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| - | '''SECRETED ASPARTIC PROTEINASE (SAP2) FROM CANDIDA ALBICANS COMPLEXED WITH A70450'''
| + | ===SECRETED ASPARTIC PROTEINASE (SAP2) FROM CANDIDA ALBICANS COMPLEXED WITH A70450=== |
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| - | ==Overview==
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| - | 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 features of a typical aspartic proteinase, it also shows some significant differences, due mainly to several sequence insertions and deletions (as revealed by homology modelling), that alter the shape of the binding cleft. There is also considerable variation in the C-terminal structural domain. CONCLUSIONS: The differences in side chains, and in the conformations adopted by the two inhibitors, particularly at their P4, P3 and P'2 positions (using standard notation for protease-inhibitor residues), allows the A70450 structure to complement, more accurately, that of the substrate-binding site of SAP2. Some differences in the binding clefts of other SAP isoenzymes may be deduced from the SAP2 structure.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8591036}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8591036 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8591036}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Candida albican]] | | [[Category: Candida albican]] |
| | [[Category: Sap2]] | | [[Category: Sap2]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:52:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:24:22 2008'' |
Revision as of 21:24, 30 June 2008
Template:STRUCTURE 1eag
SECRETED ASPARTIC PROTEINASE (SAP2) FROM CANDIDA ALBICANS COMPLEXED WITH A70450
Template:ABSTRACT PUBMED 8591036
About this Structure
1EAG is a Single protein structure of sequence from Candida albicans. Full crystallographic information is available from OCA.
Reference
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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