Sandbox Reserved 706: Difference between revisions

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* The second contact area is formed by the Rab complementarity-determining regions <scene name='Sandbox_Reserved_706/Slewyy_et_rabcdrs/1'>(RabCDRs) of Rab27B and 117-SLEWYY-122 motif of Slac2-a</scene> helical region (also see figure 4C). <ref> PMID:10025402</ref> <ref>PMID:18940604</ref>
* The second contact area is formed by the Rab complementarity-determining regions <scene name='Sandbox_Reserved_706/Slewyy_et_rabcdrs/1'>(RabCDRs) of Rab27B and 117-SLEWYY-122 motif of Slac2-a</scene> helical region (also see figure 4C). <ref> PMID:10025402</ref> <ref>PMID:18940604</ref>
At this interface, there are hydrophobic interactions and three hydrogen bonds.
At this interface, there are hydrophobic interactions and three hydrogen bonds.
Tyr121 of Slac2-a  form a hydrogen bond with the Arg90 carbonyl group of Rab27B.
<scene name='Sandbox_Reserved_706/Tyr121_arg90/1'>Tyr121 of Slac2-a  form a hydrogen bond with the Arg90</scene> carbonyl group of Rab27B.
Arg128 of Slac2-a, which is highly conserved among the Slp-family proteins, makes two hydrogen bonds with the carbonyl groups of Gln118 and Ala121 of Rab27B
Arg128 of Slac2-a, which is highly conserved among the Slp-family proteins, makes two hydrogen bonds with the carbonyl groups of Gln118 and Ala121 of Rab27B