|
|
| Line 114: |
Line 114: |
| describe any uses or application that have been made of the protein | | describe any uses or application that have been made of the protein |
|
| |
|
| ==References==
| |
| at least 5
| |
|
| |
|
|
| |
|
| Line 124: |
Line 122: |
|
| |
|
| ===Protein unfolding=== | | ===Protein unfolding=== |
| C-terminal domain<ref name="utile">PMID:20308985</ref>.
| | <ref name="utile">PMID:20308985</ref>. |
|
| |
|
| [[Image:Cow_milk.jpg |thumb|center|650px|Domain organization of ERM<ref name="utile" />]]
| |
|
| |
| A pathway of sequential unfolding (and folding) of the native 3D structure S0. SU is the coil. The U–ν links in the intermediate Sν keep their native positions and conformations (they are shown as a solid line against the background of a dotted cloud denoting the globule), whereas the other ν links (shown in dashed line) are unfolded.
| |
|
| |
| ===Contoh 2===
| |
| The FERM-tail complex represents an inactive form of the protein in which membrane protein and active binding sites are masked.<ref>doi: 10.1074/jbc.274.1.170</ref>
| |
| and α-helical domains<ref name="utile2">PMID:22012890</ref>.Conformational changes activate the proteins because they modify the intramolecular contacts, allowing them to bind to their partners. The FERM domain has a fundamental role because it allows ERM proteins to interact with integral proteins of the plasma membrane<ref>PMID:12154370</ref>.
| |
|
| |
| [[Image:Cow_milk.jpg |thumb|left|650px|Inactive ERM protein]]
| |
| [[Image:Cow_milk.jpg |thumb|right|650px|protein]]
| |
|
| |
|
| |
|
| |
| ==Specificity of contoh domain==
| |
| {{STRUCTURE_2q2m| PDB=2q2m | SCENE=| size='400'}}
| |
| As showed in the default scene, the structure 2Q2M has in total 1 Chain. These are represented by 1 sequence-unique entity. The chains A,B and C possess 9
| |
| {{Template:ColorKey_Helix}} and 15 {{Template:ColorKey_Strand}} and the chain D has only 9 {{Template:ColorKey_Helix}}and 14 {{Template:ColorKey_Strand}}. You can visualize their <scene name='Sandbox_Reserved_705/Hidoeurf/1'>repartition</scene>.
| |
|
| |
| ===Structural differences===
| |
|
| |
| More precisly,binding of the tail provokes dimerization and unfurling of the F2 motif of the FERM domain.The “closed” complex of merlin-1 is in fact an “open” dimer <ref name="utile" />. For more details about the probable quaternary states, see the [http://www.ebi.ac.uk/pdbe-srv/view/entry/3u8z/quaternary.html?global_textfield= PDBe page ]about the structure of 3u8z.
| |
|
| |
|
|
| |
|
