2baf
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FGA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= FGA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2baf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2baf OCA], [http://www.ebi.ac.uk/pdbsum/2baf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2baf RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: fibrinogen]] | [[Category: fibrinogen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:03:31 2008'' |
Revision as of 23:03, 30 March 2008
| |||||||
| Gene: | FGA (Bos taurus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 02:03:31 2008
