1a5g
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(New page: 200px<br /> <applet load="1a5g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a5g, resolution 2.06Å" /> '''HUMAN THROMBIN COMP...)
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Revision as of 18:23, 29 October 2007
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HUMAN THROMBIN COMPLEXED WITH NOVEL SYNTHETIC PEPTIDE MIMETIC INHIBITOR AND HIRUGEN
Overview
The X-ray crystal structures of four beta-strand-templated active site, inhibitors of thrombin containing P1' groups have been determined and, refined at about 2.1-A resolution to crystallographic R-values between, 0.148 and 0.164. Two of the inhibitors have an alpha-ketoamide, functionality at the scissile bond; the other two have a nonhydrolyzable, electrophilic group at the P1' position. The binding of lysine is compared, with that of arginine at the S1 specificity site, while that of, D,L-phenylalanine enantiomorphs is compared in the S3 region of thrombin., Four different P1' moieties bind at the S1' subsite in three different, ways. The binding constants vary between 2.0 microM and 70 pM. The bound, structures are used to intercorrelate the various binding constants and, also lead ... [(full description)]
About this Structure
1A5G is a [Protein complex] structure of sequences from [Hirudo medicinalis] and [Homo sapiens] with NA, BIC and EOA as [ligands]. Active as [[1]], with EC number [3.4.21.5]. Full crystallographic information is available from [OCA].
Reference
Bound structures of novel P3-P1' beta-strand mimetic inhibitors of thrombin., St Charles R, Matthews JH, Zhang E, Tulinsky A, J Med Chem. 1999 Apr 22;42(8):1376-83. PMID:10212123
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