2.0 angstrom crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region

Article Abstract:

The structure of fibronectin contains a region where a sequence composed of arginine, glysine and aspartic acid residues (or RGD loop) is located close to its 'synergy' region. Fibronectin is composed of repeating sequences of amino acids which cause the protein to twist and fold to form a structure with alternating tilted domains. The domain composed of residues 1373-1380 compose the synergy region, while the following domain contains the RGD loop at residues 1493 to 1497. The RGD region functions in cell adhesion while the synergy region is involved in the interaction of fibronectin with integrins.

Fibronectins, Protein structure

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Pathway leading to correctly folded beta-tubulin

Article Abstract:

The complete pathway leading to the generation of exchange-competent beta-tubulin is identified. ATP-dependent interaction with cytosolic chaperonin results in the production of folding intermediates which interact sequentially with four proteins. Cofactors A and D capture and stabilize beta-tubulin in a quasi-native conformation. Cofactor E, when binded to the cofactor D-beta-tubulin, interacts with cofactor C, causing the release of beta-tubulin peptides that are committed to the native state. Yeast homologs of cofactors D and E are identified through sequence analysis.

Protein folding

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FtsZ, a prokaryotic homolog of tubulin?

Article Abstract:

Sequence homology, GTP-dependent assembly, and GTP binding and hydrolysis indicate the bacterial cell division protein FtsZ to be a prokaryotic homolog of tubulin. The position of FtsZ at the central ring may lead to the binding of FtsZ to other proteins, some of which may be membrane-bound, facilitating its assembly. FtsZ is likely to participate in contractile activity involving prokaryotic kinesin or dynein.

Physiological aspects, Cell division

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