2baf
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(New page: 200px<br /><applet load="2baf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2baf" /> '''Bovine Fibrinogen alpha-C Domain'''<br /> =...)
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Revision as of 06:33, 21 November 2007
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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
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