000			02296nam a22002657a 4500
003			ZW-GwMSU
005			20250320092110.0
008			250320b |||||||| |||| 00| 0 eng d
022			_a09743626
040			_aMSU _bEnglish _cMSU _erda
050	0	0	_aQD31 JOU
100	1		_aRamakrishna, S. _eauthor
245	1	0	_aModeling the structure of SARS 3a transmembrane protein using a minimum unfavorable contact approach / _ccreated by S. Ramakrishna, Siladitya Padhi and U. Deva Priyakumar
264	1		_aBangalore : _bSpringer, _c2015.
336			_2rdacontent _atext _btxt
337			_2rdamedia _aunmediated _bn
338			_2rdacarrier _avolume _bnc
440			_aJournal of chemical sciences _vVolume 127, number 12,
520	3		_a3a is an accessory protein from SARS coronavirus that is known to play a significant role in the proliferation of the virus by forming tetrameric ion channels. Although the monomeric units are known to consist of three transmembrane (TM) domains, there are no solved structures available for the complete monomer. The present study proposes a structural model for the transmembrane region of the monomer by employing our previously tested approach, which predicts potential orientations of TM α-helices by minimizing the unfavorable contact surfaces between the different TM domains. The best model structure comprising all three α-helices has been subjected to MD simulations to examine its quality. The TM bundle was found to form a compact and stable structure with significant intermolecular interactions. The structural features of the proposed model of 3a account for observations from previous experimental investigations on the activity of the protein. Further analysis indicates that residues from the TM2 and TM3 domains are likely to line the pore of the ion channel, which is in good agreement with a recent experimental study. In the absence of an experimental structure for the protein, the proposed structure can serve as a useful model for inferring structure-function relationships about the protein.
650			_aMembrane protein modeling _vIon channel _xTransmembrane helices
700	1		_aPadhi, Siladitya _eco author
700	1		_aPriyakumar, U. Deva _eco author
856			_uhttps://doi.org/10.1007/s12039-015-0982-z
942			_2lcc _cJA
999			_c169408 _d169408