Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
p-amidinophenylmethylphosphinic acid (AMPA) was designed, synthesized and crystallized in complex with trypsin to study interactions with the oxyanion hole at the S1 site. In comparison to benzamidine, AMPA shows improved activity, which the crystal structure demonstrates to result from hydrogen bonds between the negatively charged phosphinic acid group and the catalytic residues at the oxyanion hole.
An oxyanion-hole selective serine protease inhibitor in complex with trypsin.,Cui J, Marankan F, Fu W, Crich D, Mesecar A, Johnson ME Bioorg Med Chem. 2002 Jan;10(1):41-6. PMID:11738605[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cui J, Marankan F, Fu W, Crich D, Mesecar A, Johnson ME. An oxyanion-hole selective serine protease inhibitor in complex with trypsin. Bioorg Med Chem. 2002 Jan;10(1):41-6. PMID:11738605
