1amp: Difference between revisions
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Revision as of 16:03, 26 July 2012
CRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILYCRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILY
Template:ABSTRACT PUBMED 8087555
About this StructureAbout this Structure
1amp is a 1 chain structure of Aminopeptidase with sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4][xtra 5]
- ↑ Chevrier B, Schalk C, D'Orchymont H, Rondeau JM, Moras D, Tarnus C. Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure. 1994 Apr 15;2(4):283-91. PMID:8087555
- ↑ Mahadevan D, Saldanha JW. The extracellular regions of PSMA and the transferrin receptor contain an aminopeptidase domain: implications for drug design. Protein Sci. 1999 Nov;8(11):2546-9. PMID:10595564 doi:10.1110/ps.8.11.2546
- ↑ Thomas A, Bouffioux O, Geeurickx D, Brasseur R. Pex, analytical tools for PDB files. I. GF-Pex: basic file to describe a protein. Proteins. 2001 Apr 1;43(1):28-36. PMID:11170211
- ↑ Booth RE, Lovell SC, Misquitta SA, Bateman RC Jr. Human glutaminyl cyclase and bacterial zinc aminopeptidase share a common fold and active site. BMC Biol. 2004 Feb 10;2:2. PMID:15028118 doi:10.1186/1741-7007-2-2
- ↑ Schurer G, Lanig H, Clark T. Aeromonas proteolytica aminopeptidase: an investigation of the mode of action using a quantum mechanical/molecular mechanical approach. Biochemistry. 2004 May 11;43(18):5414-27. PMID:15122907 doi:10.1021/bi0340191