Abstract:
:Drosophila projectin is an extremely large protein found within the muscle sarcomeric unit, parallel with the actin and myosin filaments. Projectin has been suggested as the elastic component of C-filaments in insect indirect flight muscles, which is consistent with its localization from the Z band to the tip of the A band in these muscles. Here, we describe the completion of the projectin sequence analysis, which defines projectin as a 1 MDa protein, composed of 39 immunoglobulin and 39 fibronectin III domains. This analysis led also to the identification of a domain rich in the amino acids P, E, V and K within the NH(2) terminus of projectin. The length of the projectin PEVK-like region varies from 100 to 624 amino acid residues, following a complex pattern of alternative splicing events. PEVK domains were first identified in vertebrate titin and they have been associated with the elasticity of the protein. The PEVK-like domain of the projectin isoforms in indirect flight muscles may contribute to the elastic function of the C-filaments. The synchronous projectin isoforms contain a PEVK-like region, and the possible non-elastic function(s) of this domain in synchronous muscles are discussed.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Southgate R,Ayme-Southgate Adoi
10.1006/jmbi.2001.5115keywords:
subject
Has Abstractpub_date
2001-11-09 00:00:00pages
1035-43issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(01)95115-0journal_volume
313pub_type
杂志文章abstract::We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 angstroms and 2.5 angstroms, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins...
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