Major vault protein: Difference between revisions

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== Structural highlights ==

MVP is highly conserved in evolution and can create the entire outer shell of the vault barrel structure, which is comprised of two identical halves. The outer shell is a closed, smooth surface without any large gaps or windows. When considering the individual MVP within a vault particle, their <scene name='78/783129/N-terminus/1'>N-terminus ( residues 113–620)</scene> forms the waist of the particle while their <scene name='78/783129/C-terminus/2'>C-terminus (residues 621-893)</scene> builds the cap and the cap/barrel junction[26]. This leads to the current belief that the N-terminus accounts for the non-covalent interactions between the identical particle halves[9]. In addition, each MVP represents a unique structure that does not share a homology with other proteins, yet exhibits a high degree of conservation [8,9,20,22,23]- around 90% within mammals [14,16].

There are several domains within MVP, among the most important is the highly conserved<scene name='78/783129/C-terminus/2'> α- helical domain</scene> near the C-terminus that functions as a coiled coil which mediates an interaction between different MVPs and subsequently vault formation. The N-terminal of MVP was reported to bind Ca2+ [+PDB], but while it has been speculated that MVP contains at least 2 Ca2+-binding EF hands in<scene name='78/783129/Ef-hand_location/1'> positions 131–143</scene>[28], substructure determinations by NMR could not confirm these EF hands and thus an alternative Ca2+ mechanism was suggested which included coordination by large number of acidic residues in the long β1/β2 and β2/β3 loops of multiple MVP domains [10 find PBD], in a way similar to that which is found in integrins(figure x).

There are several domains within MVP, among the most important is the highly conserved<scene name='78/783129/C-terminus/2'> α- helical domain</scene> near the C-terminus that functions as a coiled coil which mediates an interaction between different MVPs and subsequently vault formation. The N-terminal of MVP was reported to bind Ca2+ [+PDB], but while it has been speculated that MVP contains at least 2 Ca2+-binding EF hands in<scene name='78/783129/Ef-hand_location/1'> positions 131–143</scene>[28], substructure determinations by NMR could not confirm these EF hands and thus an alternative Ca2+ mechanism was suggested which included coordination by large number of <scene name='78/783129/Beta_loops/1'>acidic residues in the long β1/β2 and β2/β3 loops</scene> of multiple MVP domains [10 find PBD], in a way similar to that which is found in integrins(figure x).

==The MVP gene, transcription, translation and post translation modifications==

Major vault protein: Difference between revisions

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 == Structural highlights ==
 MVP is highly conserved in evolution and can create the entire outer shell of the vault barrel structure, which is comprised of two identical halves. The outer shell is a closed, smooth surface without any large gaps or windows. When considering the individual MVP within a vault particle, their <scene name='78/783129/N-terminus/1'>N-terminus ( residues 113–620)</scene> forms the waist of the particle while their <scene name='78/783129/C-terminus/2'>C-terminus (residues 621-893)</scene> builds the cap and the cap/barrel junction[26]. This leads to the current belief that the N-terminus accounts for the non-covalent interactions between the identical particle halves[9]. In addition, each MVP represents a unique structure that does not share a homology with other proteins, yet exhibits a high degree of conservation [8,9,20,22,23]- around 90% within mammals [14,16].
-There are several domains within MVP, among the most important is the highly conserved<scene name='78/783129/C-terminus/2'> α- helical domain</scene> near the C-terminus that functions as a coiled coil which mediates an interaction between different MVPs and subsequently vault formation. The N-terminal of MVP was reported to bind Ca2+ [+PDB], but while it has been speculated that MVP contains at least 2 Ca2+-binding EF hands in<scene name='78/783129/Ef-hand_location/1'> positions 131–143</scene>[28], substructure determinations by NMR could not confirm these EF hands and thus an alternative Ca2+ mechanism was suggested which included coordination by large number of acidic residues in the long β1/β2 and β2/β3 loops of multiple MVP domains [10 find PBD], in a way similar to that which is found in integrins(figure x).
+There are several domains within MVP, among the most important is the highly conserved<scene name='78/783129/C-terminus/2'> α- helical domain</scene> near the C-terminus that functions as a coiled coil which mediates an interaction between different MVPs and subsequently vault formation. The N-terminal of MVP was reported to bind Ca2+ [+PDB], but while it has been speculated that MVP contains at least 2 Ca2+-binding EF hands in<scene name='78/783129/Ef-hand_location/1'> positions 131–143</scene>[28], substructure determinations by NMR could not confirm these EF hands and thus an alternative Ca2+ mechanism was suggested which included coordination by large number of <scene name='78/783129/Beta_loops/1'>acidic residues in the long β1/β2 and β2/β3 loops</scene> of multiple MVP domains [10 find PBD], in a way similar to that which is found in integrins(figure x).
 ==The MVP gene, transcription, translation and post translation modifications==