1dtl is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cardiac troponin C (cTnC) is the calcium-dependent switch for contraction in heart muscle and a potential target for drugs in the therapy of congestive heart failure. This calmodulin-like protein consists of two lobes connected by a central linker; each lobe contains two EF-hand domains. The regulatory N-terminal lobe of cTnC, unlike that of skeletal troponin C (sTnC), contains only one functional EF-hand and does not open fully upon the binding of Ca(2+). We have determined the crystal structure of cTnC, with three bound Ca(2+) ions, complexed with the calcium-sensitizer bepridil, to 2.15-A resolution. In contrast to apo- and 3Ca(2+)-cTnC, the drug-bound complex displays a fully open N-terminal lobe similar to the N-terminal lobes of 4Ca(2+)-sTnC and cTnC bound to a C-terminal fragment of cardiac troponin I (residues 147-163). The closing of the lobe is sterically hindered by one of the three bound bepridils. Our results provide a structural basis for the Ca(2+)-sensitizing effect of bepridil and reveal the details of a distinctive two-stage mechanism for Ca(2+) regulation by troponin C in cardiac muscle.
Bepridil opens the regulatory N-terminal lobe of cardiac troponin C.,Li Y, Love ML, Putkey JA, Cohen C Proc Natl Acad Sci U S A. 2000 May 9;97(10):5140-5. PMID:10792039[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Li Y, Love ML, Putkey JA, Cohen C. Bepridil opens the regulatory N-terminal lobe of cardiac troponin C. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5140-5. PMID:10792039 doi:http://dx.doi.org/10.1073/pnas.090098997
