Ontology highlight
ABSTRACT:
SUBMITTER: Mikulski R
PROVIDER: S-EPMC3223279 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature
Mikulski Rose R Domsic John F JF Ling George G Tu Chingkuang C Robbins Arthur H AH Silverman David N DN McKenna Robert R
Archives of biochemistry and biophysics 20111005 2
The tryptophan residue Trp5, highly conserved in the α class of carbonic anhydrases including human carbonic anhydrase II (HCA II), is positioned at the entrance of the active site cavity and forms a π-stacking interaction with the imidazole ring of the proton shuttle His64 in its outward orientation. We have observed that replacement of Trp5 in HCA II caused significant structural changes, as determined by X-ray diffraction, in the conformation of 11 residues at the N-terminus and in the orient ...[more]