2BAF
Bovine Fibrinogen alpha-C Domain
Summary for 2BAF
| Entry DOI | 10.2210/pdb2baf/pdb |
| NMR Information | BMRB: 6893 |
| Descriptor | Fibrinogen alpha chain (1 entity in total) |
| Functional Keywords | fibrinogen, beta hairpin, blood clotting |
| Biological source | Bos taurus (cattle) |
| Cellular location | Secreted: P02672 |
| Total number of polymer chains | 1 |
| Total formula weight | 18152.63 |
| Authors | Burton, R.A. (deposition date: 2005-10-14, release date: 2006-02-28, Last modification date: 2024-10-16) |
| Primary citation | Burton, R.A.,Tsurupa, G.,Medved, L.,Tjandra, N. Identification of an Ordered Compact Structure within the Recombinant Bovine Fibrinogen alphaC-Domain Fragment by NMR. Biochemistry, 45:2257-2266, 2006 Cited by PubMed Abstract: 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. PubMed: 16475814DOI: 10.1021/bi052380c PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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