Sandbox Reserved 706: Difference between revisions

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There are three contact areas in the interface between Rab27B and Slac2-a. The first and second contact areas involve the coiled-coil regions of Slac2-a and constitute the main interface.

[[Image:Rab27B slac2a image3.gif | 200 px | thumb | left |Picture 3: Caption: ]]

*The first contact area of the Rab27B/Slac2-a interface consists of <scene name='Sandbox_Reserved_706/6a9_rabcdr/2'> residues 6 to 9 from the Rab complementarity-determining regions (RabCDR)</scene> , part of the switch and interswitch regions of Rab27B, and the coiled-coil regions of Slac2-a.<ref>PMID:18940604</ref> In this first contact area we can find three different types of interactions, electrostatic, hydrophobic and hydrogen bonds: (see figure 3A)

*The first contact area of the Rab27B/Slac2-a interface consists of <scene name='Sandbox_Reserved_706/6a9_rabcdr/2'> residues 6 to 9 from the Rab complementarity-determining regions (RabCDR)</scene> , part of the switch and interswitch regions of Rab27B, and the coiled-coil regions of Slac2-a.<ref>PMID:18940604</ref> In this first contact area we can find three different types of interactions, electrostatic, hydrophobic and hydrogen bonds: (see figure 4A)

-<scene name='Sandbox_Reserved_706/Phe81_leu84_phe88/1'>Phe81, Leu84, and Phe88</scene> from <scene name='Sandbox_Reserved_706/Switch2_rab27b/1'>switch 2</scene> of Rab27B participate in {{Template:ColorKey_Hydrophobic}} interactions with the residues from <scene name='Sandbox_Reserved_706/Alpha_5_et_1_de_slac2/1'>α1 and α5</scene> of Slac2-a.

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To finish, <scene name='Sandbox_Reserved_706/Glu32_tyr6/1'>Glu32 of Slac2-a forms a hydrogen bond with Tyr6 of Rab27B</scene>. <ref>PMID:18940604</ref>

* The second contact area is formed by the Rab complementarity-determining regions (RabCDRs) of Rab27B and 117-SLEWYY-122 motif of Slac2-a helical region (also see ~~Figure 6C~~). <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.

Tyr121 of Slac2-a form a hydrogen bond with the Arg90 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

* The third contact area is the smallest one . It involves the zinc-binding subdomain of Slac2-a and the b2–b3 loop of Rab27B, with superposition of their molecular surfaces. (See figure 3E)

* The third contact area is the smallest one . It involves the zinc-binding subdomain of Slac2-a and the b2–b3 loop of Rab27B, with superposition of their molecular surfaces. (See figure 4E)

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@@ Line 112: / Line 112: @@
 There are three contact areas in the interface between Rab27B and Slac2-a.  The first and second contact areas involve the coiled-coil regions of Slac2-a and constitute the main interface.
 [[Image:Rab27B slac2a image3.gif | 200 px | thumb | left |Picture 3:   Caption: ]]
-*The first contact area of the Rab27B/Slac2-a interface consists of <scene name='Sandbox_Reserved_706/6a9_rabcdr/2'> residues 6 to 9 from  the Rab complementarity-determining regions (RabCDR)</scene> , part of the switch and interswitch regions of Rab27B, and the coiled-coil regions of Slac2-a.<ref>PMID:18940604</ref> In this first contact area we can find three different types of interactions, electrostatic, hydrophobic and hydrogen bonds: (see figure 3A)
+*The first contact area of the Rab27B/Slac2-a interface consists of <scene name='Sandbox_Reserved_706/6a9_rabcdr/2'> residues 6 to 9 from  the Rab complementarity-determining regions (RabCDR)</scene> , part of the switch and interswitch regions of Rab27B, and the coiled-coil regions of Slac2-a.<ref>PMID:18940604</ref> In this first contact area we can find three different types of interactions, electrostatic, hydrophobic and hydrogen bonds: (see figure 4A)
 -<scene name='Sandbox_Reserved_706/Phe81_leu84_phe88/1'>Phe81, Leu84, and Phe88</scene> from <scene name='Sandbox_Reserved_706/Switch2_rab27b/1'>switch 2</scene> of Rab27B participate in {{Template:ColorKey_Hydrophobic}} interactions with the residues from <scene name='Sandbox_Reserved_706/Alpha_5_et_1_de_slac2/1'>α1 and α5</scene> of Slac2-a.
@@ Line 127: / Line 127: @@
 To finish, <scene name='Sandbox_Reserved_706/Glu32_tyr6/1'>Glu32 of Slac2-a forms a hydrogen bond with Tyr6 of Rab27B</scene>. <ref>PMID:18940604</ref>
-* The second contact area is formed by the Rab complementarity-determining regions (RabCDRs) of Rab27B and 117-SLEWYY-122 motif of Slac2-a helical region (also see Figure 6C). <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.
 Tyr121 of Slac2-a  form a hydrogen bond with the Arg90 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
-* The third contact area is the smallest one . It  involves the zinc-binding subdomain of Slac2-a and the b2–b3 loop of Rab27B, with superposition of their molecular surfaces. (See figure 3E)
+* The third contact area is the smallest one . It  involves the zinc-binding subdomain of Slac2-a and the b2–b3 loop of Rab27B, with superposition of their molecular surfaces. (See figure 4E)