<p><img width="180" height="135" align="left" alt="" src="/userfiles/image/Asif%20Khan.jpg" style="MARGIN-RIGHT: 10px" /></p>
<h3>Type the title here</h3>
<p>Gag itself is sufficient for immature-particle assembly. The   interactions critical for immature-particle assembly are mediated by   CA-CA and NC-RNA interfaces. CA consists of two subdomains, the   CA&ndash;N-terminal domain (NTD) and the CA&ndash;C-terminal domain (CTD), connected   by a short sequence. Despite a low level of sequence homology, all   available retroviral CA-NTD structures show conserved structural motifs   consisting of six or seven &alpha;-helices and an N-terminal &beta;-hairpin   anchored by a salt bridge between the N-terminal proline and an   aspartate in helix 3.</p>
<p>The assembly of fully infectious retroviruses comprises two different   phases: immature- and mature-particle formation. Initially, the virus   is formed in immature form by self-association of the major structural   polyprotein Gag into spherical particles either at the plasma membrane   (alpharetroviruses, gammaretroviruses, or lentiviruses) or at a  distinct  site within the infected cell (betaretroviruses). The  particles are  organized by lattices of Gag and Gag-derived polyproteins  that associate  with the plasma membrane that becomes the outer layer  of the immature  particle released during budding. Upon release from the  host cell, the  Gag precursor is proteolytically processed into  N-terminal membrane  binding matrix protein (MA), two-domain capsid  protein (CA), and  RNA-binding nucleocapsid protein (NC). This cleavage  leads to a dramatic  morphological change and reorganization of the  virus particle from its  immature form into a mature, infectious virion.</p>
<h3>Type the title here</h3>
<p><img width="180" height="135" align="left" alt="" src="/userfiles/image/Asif%20Khan.jpg" style="MARGIN-RIGHT: 10px" /></p>
<p>Gag itself is sufficient for immature-particle assembly. The    interactions critical for immature-particle assembly are mediated by    CA-CA and NC-RNA interfaces. CA consists of two subdomains, the    CA&ndash;N-terminal domain (NTD) and the CA&ndash;C-terminal domain (CTD), connected    by a short sequence. Despite a low level of sequence homology, all    available retroviral CA-NTD structures show conserved structural motifs    consisting of six or seven &alpha;-helices and an N-terminal &beta;-hairpin    anchored by a salt bridge between the N-terminal proline and an    aspartate in helix 3.</p>
<p>The assembly of fully infectious retroviruses comprises two different    phases: immature- and mature-particle formation. Initially, the virus    is formed in immature form by self-association of the major  structural   polyprotein Gag into spherical particles either at the  plasma membrane   (alpharetroviruses, gammaretroviruses, or  lentiviruses) or at a  distinct  site within the infected cell  (betaretroviruses). The  particles are  organized by lattices of Gag and  Gag-derived polyproteins  that associate  with the plasma membrane that  becomes the outer layer  of the immature  particle released during  budding. Upon release from the  host cell, the  Gag precursor is  proteolytically processed into  N-terminal membrane  binding matrix  protein (MA), two-domain capsid  protein (CA), and  RNA-binding  nucleocapsid protein (NC). This cleavage  leads to a dramatic   morphological change and reorganization of the  virus particle from its   immature form into a mature, infectious virion.</p>
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