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. Author manuscript; available in PMC: 2009 May 11.
Published in final edited form as: J Biol Chem. 2006 Sep 13;281(46):35478–35486. doi: 10.1074/jbc.M607204200

FIGURE 4. Structure of V317C/T401C AT from a different crystal form reveals similar RCL conformation and contacts.

FIGURE 4

A, stereo view of a ribbon diagram of the AT (colored as before), heparin (ball-and-stick), and S195A thrombin (semitransparent magenta and pink) complex. The RCL is clearly in a native-like conformation despite the presence of bound heparin. Two thrombin molecules bind to either side of the same site on heparin, and their active sites are occupied by the C terminus of adjacent light chains. B, the RCLs of native AT from the heterodimer (cyan) is compared with those of the V317C/T401C variant in the monomeric form (yellow) and in its nonproductive thrombin complex (magenta). The RCLs are shown from hinge region residue P14 (bottom) to P6′ (top).