Alpha crystallin: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
<Structure load='3L1E' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | |||
== Function == | == Function == | ||
| Line 19: | Line 20: | ||
Alpha-A crystallin is made of 173 amino acids arranged in <scene name='88/881544/Beta_sheet/1'>a beta sheet pattern</scene>. The molecular mass of the alpha-A subunit is 19.8 kDa, and the homooligomer weighs 660 kDa. On the other hand, Alpha-B crystallin has 165 amino acids arranged in seven beta-sheets, has a molecular mass of 20 kDa, and its homooligomer weight is 620 kDa. Together, the alpha-crystallin protein has four Zinc binding sites, all of which are in the same position as the four metal-binding sites. Within the crystallin is two tryptophan residues, Trp9 and Trp60, both of which can be found in the alpha-B crystallin subunit. | Alpha-A crystallin is made of 173 amino acids arranged in <scene name='88/881544/Beta_sheet/1'>a beta sheet pattern</scene>. The molecular mass of the alpha-A subunit is 19.8 kDa, and the homooligomer weighs 660 kDa. On the other hand, Alpha-B crystallin has 165 amino acids arranged in seven beta-sheets, has a molecular mass of 20 kDa, and its homooligomer weight is 620 kDa. Together, the alpha-crystallin protein has four Zinc binding sites, all of which are in the same position as the four metal-binding sites. Within the crystallin is two tryptophan residues, Trp9 and Trp60, both of which can be found in the alpha-B crystallin subunit. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||