1w9p: Difference between revisions

Revision as of 01:45, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1w9p.png

Template:STRUCTURE 1w9p

SPECIFICITY AND AFFINITY OF NATURAL PRODUCT CYCLOPENTAPEPTIDE INHIBITORS AGAINST ASPERGILLUS FUMIGATUS, HUMAN AND BACTERIAL CHITINASEFRASPECIFICITY AND AFFINITY OF NATURAL PRODUCT CYCLOPENTAPEPTIDE INHIBITORS AGAINST ASPERGILLUS FUMIGATUS, HUMAN AND BACTERIAL CHITINASEFRA

Template:ABSTRACT PUBMED 15664516

About this StructureAbout this Structure

1W9P is a Single protein structure of sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA.

ReferenceReference

Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases., Rao FV, Houston DR, Boot RG, Aerts JM, Hodkinson M, Adams DJ, Shiomi K, Omura S, van Aalten DM, Chem Biol. 2005 Jan;12(1):65-76. PMID:15664516

Page seeded by OCA on Tue Jul 29 01:45:12 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1w9p.jpg|left|200px]]
+{{Seed}}
+[[Image:1w9p.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1w9p|  PDB=1w9p  |  SCENE=  }}
-'''SPECIFICITY AND AFFINITY OF NATURAL PRODUCT CYCLOPENTAPEPTIDE INHIBITORS AGAINST ASPERGILLUS FUMIGATUS, HUMAN AND BACTERIAL CHITINASEFRA'''
+===SPECIFICITY AND AFFINITY OF NATURAL PRODUCT CYCLOPENTAPEPTIDE INHIBITORS AGAINST ASPERGILLUS FUMIGATUS, HUMAN AND BACTERIAL CHITINASEFRA===
-==Overview==
+<!--
-Family 18 chitinases play key roles in organisms ranging from bacteria to man. There is a need for specific, potent inhibitors to probe the function of these chitinases in different organisms. Such molecules could also provide leads for the development of chemotherapeuticals with fungicidal, insecticidal, or anti-inflammatory potential. Recently, two natural product peptides, argifin and argadin, have been characterized, which structurally mimic chitinase-chitooligosaccharide interactions and inhibit a bacterial chitinase in the nM-mM range. Here, we show that these inhibitors also act on human and Aspergillus fumigatus chitinases. The structures of these enzymes in complex with argifin and argadin, together with mutagenesis, fluorescence, and enzymology, reveal that subtle changes in the binding site dramatically affect affinity and selectivity. The data show that it may be possible to develop specific chitinase inhibitors based on the argifin/argadin scaffolds.
+The line below this paragraph, {{ABSTRACT_PUBMED_15664516}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15664516 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15664516}}
 ==About this Structure==
@@ Line 38: / Line 42: @@
 [[Category: Hydrolase]]
 [[Category: Peptide inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:21:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:45:12 2008''