Introduction to protein structure: Difference between revisions
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'''Cys''' - X<sub>(2-4)</sub> - '''Cys''' - X<sub>(3)</sub> - Phe - X<sub>(5)</sub> - Leu - X<sub>(2)</sub> - '''His''' - X<sub>(3)</sub> - '''His''' <br/> | '''Cys''' - X<sub>(2-4)</sub> - '''Cys''' - X<sub>(3)</sub> - Phe - X<sub>(5)</sub> - Leu - X<sub>(2)</sub> - '''His''' - X<sub>(3)</sub> - '''His''' <br/> | ||
<br | <br | ||
The example structure shown to <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_highlight/1'>illustrate the motif</scene> is that of Zif268 protein-DNA complex from Mus musculus (PDB entry 1AAY). In this example (a C2H2 class zinc finger) the conserved <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_cysteine/1'>cysteine</scene> and <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_histidine/2'>histidine</scene> residues form ligands to a <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_zn/1'>zinc ion</scene> whose coordination is essential to stabilise the tertiary fold of the protein. The fold is important because it helps orientate the <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_recognition/1'>recognition helices</scene> to bind to the <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_major_groove/1'>major groove of the DNA</scene>. | The example structure shown to <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_highlight/1'>illustrate the motif</scene> is that of Zif268 protein-DNA complex from Mus musculus (PDB entry 1AAY). In this example (a C2H2 class zinc finger) the conserved <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_cysteine/1'>cysteine</scene> and <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_histidine/2'>histidine</scene> residues form ligands to a <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_zn/1'>zinc ion</scene> whose coordination is essential to stabilise the tertiary fold of the protein. The fold is important because it helps orientate the <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_recognition/1'>recognition helices</scene> to bind to the <scene name='User:James_D_Watson/Structural_Templates/Zinc_finger_major_groove/1'>major groove of the DNA</scene>. | ||
{{Clear}} | {{Clear}} | ||
==Domain== | |||
A domain is an independently folded region of a protein that has a particular function. In contrast to motifs, domains can exist as separate, functional proteins. Often domains of proteins have different functions. For example, [[glyceraldehyde-3-phosphate dehydrogenase]] has <scene name='57/575866/G3pd_domains/1'>two domains</scene>: a NAD+ binding domain and a glyceraldehyde-3-phosphate binding domain. The NAD binding domain is | |||
==Tertiary Structure== | ==Tertiary Structure== | ||
