Atragin: Difference between revisions

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'''Disintegrin-like Domain ''

Following the M domain and a linker <scene name='Atragin/S-region/1'>S-region</scene>, is the <scene name='Atragin/D_arm_shoulder/1'>Disintegrin-like</scene>(D) domain. This domain is thought to play an important role in the relative orientation of the M and C domains in P-III SVMPs (Think back to C-shaped versus I-shaped). Atragin maintains the C-shaped architecture as its <scene name='Atragin/D_arm_ssbond/2'>D-shoulder</scene> domain has three disulfide bonds, and its <scene name='Atragin/D_arm_ssbond/1'>D-arm domain</scene> conatins another 3 disulfide bonds, which is similar to other C-shaped proteins <ref name=Igarashi>PMID: 17485084</ref><ref name=Takeda>PMID: 16688218</ref>. One <scene name='Atragin/D_arm_shoulder_ssbond/2'>disulfide bond</scene> also connects these two subdomains.

Following the M domain and a linker <scene name='Atragin/S-region/1'>S-region</scene>, is the <scene name='Atragin/D_arm_shoulder/1'>Disintegrin-like</scene>(D) domain. This domain is thought to play an important role in the relative orientation of the M and C domains in P-III SVMPs (Think back to C-shaped versus I-shaped). Atragin maintains the C-shaped architecture as its <scene name='Atragin/D_arm_ssbond/2'>D-shoulder</scene> domain has three disulfide bonds, and its <scene name='Atragin/D_arm_ssbond/1'>D-arm domain</scene> conatins another 3 disulfide bonds, which is similar to other C-shaped proteins <ref name=Igarashi>PMID: 17485084</ref><ref name=Takeda>PMID: 16688218</ref>. These multiple disulfide bonds make the protein structure very stable. One <scene name='Atragin/D_arm_shoulder_ssbond/2'>disulfide bond</scene> also connects these two subdomains.

The disulfide bond pattern in the D domain alters the orientations of the <scene name='Atragin/All_domains/1'>other domains</scene> in the ADAM/adamalysin/ reprolysins family <ref name=Guan>PMID: 19932752</ref>. The different orientations could explain some of the ADAM enzymatic processes, seeing as the different lengths or altering the disulfide pairs of the D-domain can increase or decrease the size of the cleft and the orientation. This could cause for substrates of different sizes and shapes to able to be cleaved by the M-domain in ADAMs <ref name=Guan>PMID: 19932752</ref>.

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'''Cysteine-rich Domain ''

The Cysteine-rich (C) domain contains the <scene name='Atragin/C_wristahnd/1'>C-wrist and C-hand </scene>domains. The C-hand subdomain is the most intriguing to most researches because it contains the Hyper Variable Region (HVR<scene name='Atragin/Hvr/1'>Hyper Variable Region (HVR)</scene>. This region is through to play an important role in target selection since it sits on the inside of the C-shaped structures cleft <ref name=Takeda>PMID: 16688218</ref>. The C domain of Atragin consists of seven <scene name='Atragin/C_ssbonds/1'>disulfide bonds</scene>, and this suggests it may play a functional role. The HVR of Atragin is also though to be responsible for the inhibitory affect on cell migration activity <ref name=Guan>PMID: 19932752</ref>.

The Cysteine-rich (C) domain contains the <scene name='Atragin/C_wristahnd/1'>C-wrist and C-hand </scene>domains. The C-hand subdomain is the most intriguing to most researches because it contains the Hyper Variable Region (HVR<scene name='Atragin/Hvr/1'>Hyper Variable Region (HVR)</scene>. This region is through to play an important role in target selection since it sits on the inside of the C-shaped structures cleft <ref name=Takeda>PMID: 16688218</ref>. The C domain of Atragin consists of seven <scene name='Atragin/C_ssbonds/1'>disulfide bonds</scene>, and this suggests it may play a functional role. The HVR of Atragin is also though to be responsible for the inhibitory affect on cell migration activity since it is exposed to target recognition <ref name=Guan>PMID: 19932752</ref>.

</StructureSection>

==References==

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@@ Line 19: / Line 19: @@
 '''Disintegrin-like Domain ''
-Following the M domain and a linker <scene name='Atragin/S-region/1'>S-region</scene>, is the  <scene name='Atragin/D_arm_shoulder/1'>Disintegrin-like</scene>(D) domain. This domain is thought to play an important role in the relative orientation of the M and C domains in P-III SVMPs (Think back to C-shaped versus I-shaped). Atragin maintains the C-shaped architecture as its <scene name='Atragin/D_arm_ssbond/2'>D-shoulder</scene> domain has three disulfide bonds, and its <scene name='Atragin/D_arm_ssbond/1'>D-arm domain</scene> conatins another 3 disulfide bonds, which is similar to other C-shaped proteins <ref name=Igarashi>PMID: 17485084</ref><ref name=Takeda>PMID: 16688218</ref>.  One <scene name='Atragin/D_arm_shoulder_ssbond/2'>disulfide bond</scene> also connects these two subdomains.
+Following the M domain and a linker <scene name='Atragin/S-region/1'>S-region</scene>, is the  <scene name='Atragin/D_arm_shoulder/1'>Disintegrin-like</scene>(D) domain. This domain is thought to play an important role in the relative orientation of the M and C domains in P-III SVMPs (Think back to C-shaped versus I-shaped). Atragin maintains the C-shaped architecture as its <scene name='Atragin/D_arm_ssbond/2'>D-shoulder</scene> domain has three disulfide bonds, and its <scene name='Atragin/D_arm_ssbond/1'>D-arm domain</scene> conatins another 3 disulfide bonds, which is similar to other C-shaped proteins <ref name=Igarashi>PMID: 17485084</ref><ref name=Takeda>PMID: 16688218</ref>. These multiple disulfide bonds make the protein structure very stable.  One <scene name='Atragin/D_arm_shoulder_ssbond/2'>disulfide bond</scene> also connects these two subdomains.
 The disulfide bond pattern in the D domain alters the orientations of the <scene name='Atragin/All_domains/1'>other domains</scene> in the ADAM/adamalysin/ reprolysins family <ref name=Guan>PMID: 19932752</ref>. The different orientations could explain some of the ADAM enzymatic processes, seeing as the different lengths or altering the disulfide pairs of the D-domain can increase or decrease the size of the cleft and the orientation. This could cause for substrates of different sizes and shapes to able to be cleaved by the M-domain in ADAMs <ref name=Guan>PMID: 19932752</ref>.
@@ Line 25: / Line 25: @@
 '''Cysteine-rich Domain ''
-The Cysteine-rich (C) domain contains the <scene name='Atragin/C_wristahnd/1'>C-wrist and C-hand </scene>domains. The C-hand subdomain is the most intriguing to most researches because it contains the Hyper Variable Region (HVR<scene name='Atragin/Hvr/1'>Hyper Variable Region (HVR)</scene>. This region is through to play an important role in target selection since it sits on the inside of the C-shaped structures cleft <ref name=Takeda>PMID: 16688218</ref>. The C domain of Atragin consists of seven <scene name='Atragin/C_ssbonds/1'>disulfide bonds</scene>, and this suggests it may play a functional role.  The HVR of Atragin is also though to be responsible for the inhibitory affect on cell migration activity <ref name=Guan>PMID: 19932752</ref>.
+The Cysteine-rich (C) domain contains the <scene name='Atragin/C_wristahnd/1'>C-wrist and C-hand </scene>domains. The C-hand subdomain is the most intriguing to most researches because it contains the Hyper Variable Region (HVR<scene name='Atragin/Hvr/1'>Hyper Variable Region (HVR)</scene>. This region is through to play an important role in target selection since it sits on the inside of the C-shaped structures cleft <ref name=Takeda>PMID: 16688218</ref>. The C domain of Atragin consists of seven <scene name='Atragin/C_ssbonds/1'>disulfide bonds</scene>, and this suggests it may play a functional role.  The HVR of Atragin is also though to be responsible for the inhibitory affect on cell migration activity since it is exposed to target recognition <ref name=Guan>PMID: 19932752</ref>.
 </StructureSection>
 ==References==
 {{Reflist}}