2baf
From Proteopedia
Bovine Fibrinogen alpha-C Domain
Overview
The NMR solution structure of the bovine fibrinogen alphaC-domain fragment, including residues Aalpha374-538, reveals a type-I' beta-hairpin, restricted at the base by a C423-C453 disulfide linkage and a short turn preceding C423. Although both faces of the hairpin are formed mainly by hydrophilic residues, one of them is uncharged while the other has a characteristic pattern of charged residues which are highly conserved among vertebrate species. Chemical shift indexing and relaxation data indicate the presence of a collapsed hydrophobic region next to the hairpin that includes approximately 30 residues with slower concerted motion and higher content of nonpolar residues and, according to a previous study (Tsurupa, G., Tsonev, L., and Medved, L. (2002) Biochemistry 41, 6449-6459), may cooperate with the hairpin to form a compact cooperative unit (domain). Structure and relaxation data show that the region between C423 and C453 is populated by both random coil and beta-structure, suggesting that the cooperative structure in the isolated alphaC-domain is intrinsically unstable. This observation is in agreement with a very low energy of stabilization of the Aalpha374-538 fragment determined in unfolding experiments. The low stability of the alphaC-domain suggests a possible explanation for the previously observed intra- and intermolecular interactions of these domains in fibrinogen and fibrin.
About this Structure
2BAF is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR., Burton RA, Tsurupa G, Medved L, Tjandra N, Biochemistry. 2006 Feb 21;45(7):2257-66. PMID:16475814 Page seeded by OCA on Sat May 3 20:02:27 2008
