- ข้อความ
- ประวัติศาสตร์
ABSTRACT: Apolipoprotein AI (apoA-I
ABSTRACT: Apolipoprotein AI (apoA-I) is the principal
acceptor of lipids from ATP-binding cassette transporter A1, a
process that yields nascent high density lipoproteins. Analysis
of lipidated apoA-I conformation yields a belt or twisted belt in
which two strands of apoA-I lie antiparallel to one another. In
contrast, biophysical studies have suggested that a part of lipidfree apoA-I was arranged in a four-helix bundle. To understand
how lipid-free apoA-I opens from a bundle to a belt while
accepting lipid it was necessary to have a more refined model
for the conformation of lipid-free apoA-I. This study reports
the conformation of lipid-free human apoA-I using lysine-tolysine chemical cross-linking in conjunction with disulfide
cross-linking achieved using selective cysteine mutations. After
proteolysis, cross-linked peptides were verified by sequencing using tandem mass spectrometry. The resulting structure is
compact with roughly four helical regions, amino acids 44−186, bundled together. C- and N-terminal ends, amino acids 1−43
and 187−243, respectively, are folded such that they lie close to one another. An unusual feature of the molecule is the high
degree of connectivity of lysine40 with six other lysines, lysines that are close, for example, lysine59, to distant lysines, for example,
lysine239, that are at the opposite end of the primary sequence. These results are compared and contrasted with other reported
conformations for lipid-free human apoA-I and an NMR study of mouse apoA-I.
acceptor of lipids from ATP-binding cassette transporter A1, a
process that yields nascent high density lipoproteins. Analysis
of lipidated apoA-I conformation yields a belt or twisted belt in
which two strands of apoA-I lie antiparallel to one another. In
contrast, biophysical studies have suggested that a part of lipidfree apoA-I was arranged in a four-helix bundle. To understand
how lipid-free apoA-I opens from a bundle to a belt while
accepting lipid it was necessary to have a more refined model
for the conformation of lipid-free apoA-I. This study reports
the conformation of lipid-free human apoA-I using lysine-tolysine chemical cross-linking in conjunction with disulfide
cross-linking achieved using selective cysteine mutations. After
proteolysis, cross-linked peptides were verified by sequencing using tandem mass spectrometry. The resulting structure is
compact with roughly four helical regions, amino acids 44−186, bundled together. C- and N-terminal ends, amino acids 1−43
and 187−243, respectively, are folded such that they lie close to one another. An unusual feature of the molecule is the high
degree of connectivity of lysine40 with six other lysines, lysines that are close, for example, lysine59, to distant lysines, for example,
lysine239, that are at the opposite end of the primary sequence. These results are compared and contrasted with other reported
conformations for lipid-free human apoA-I and an NMR study of mouse apoA-I.
0/5000
ABSTRACT: Apolipoprotein AI (apoA-I) is the principal
acceptor of lipids from ATP-binding cassette transporter A1, a
process that yields nascent high density lipoproteins. Analysis
of lipidated apoA-I conformation yields a belt or twisted belt in
which two strands of apoA-I lie antiparallel to one another. In
contrast, biophysical studies have suggested that a part of lipidfree apoA-I was arranged in a four-helix bundle. To understand
how lipid-free apoA-I opens from a bundle to a belt while
accepting lipid it was necessary to have a more refined model
for the conformation of lipid-free apoA-I. This study reports
the conformation of lipid-free human apoA-I using lysine-tolysine chemical cross-linking in conjunction with disulfide
cross-linking achieved using selective cysteine mutations. After
proteolysis, cross-linked peptides were verified by sequencing using tandem mass spectrometry. The resulting structure is
compact with roughly four helical regions, amino acids 44−186, bundled together. C- and N-terminal ends, amino acids 1−43
and 187−243, respectively, are folded such that they lie close to one another. An unusual feature of the molecule is the high
degree of connectivity of lysine40 with six other lysines, lysines that are close, for example, lysine59, to distant lysines, for example,
lysine239, that are at the opposite end of the primary sequence. These results are compared and contrasted with other reported
conformations for lipid-free human apoA-I and an NMR study of mouse apoA-I.
acceptor of lipids from ATP-binding cassette transporter A1, a
process that yields nascent high density lipoproteins. Analysis
of lipidated apoA-I conformation yields a belt or twisted belt in
which two strands of apoA-I lie antiparallel to one another. In
contrast, biophysical studies have suggested that a part of lipidfree apoA-I was arranged in a four-helix bundle. To understand
how lipid-free apoA-I opens from a bundle to a belt while
accepting lipid it was necessary to have a more refined model
for the conformation of lipid-free apoA-I. This study reports
the conformation of lipid-free human apoA-I using lysine-tolysine chemical cross-linking in conjunction with disulfide
cross-linking achieved using selective cysteine mutations. After
proteolysis, cross-linked peptides were verified by sequencing using tandem mass spectrometry. The resulting structure is
compact with roughly four helical regions, amino acids 44−186, bundled together. C- and N-terminal ends, amino acids 1−43
and 187−243, respectively, are folded such that they lie close to one another. An unusual feature of the molecule is the high
degree of connectivity of lysine40 with six other lysines, lysines that are close, for example, lysine59, to distant lysines, for example,
lysine239, that are at the opposite end of the primary sequence. These results are compared and contrasted with other reported
conformations for lipid-free human apoA-I and an NMR study of mouse apoA-I.
การแปล กรุณารอสักครู่..
ABSTRACT: Apolipoprotein AI (apoA-I) is the principal
acceptor of lipids from ATP-binding cassette transporter A1, a
process that yields nascent high density lipoproteins. Analysis
of lipidated apoA-I conformation yields a belt or twisted belt in
which two strands of apoA-I lie antiparallel to one another. In
contrast, biophysical studies have suggested that a part of lipidfree apoA-I was arranged in a four-helix bundle. To understand
how lipid-free apoA-I opens from a bundle to a belt while
accepting lipid it was necessary to have a more refined model
for the conformation of lipid-free apoA-I. This study reports
the conformation of lipid-free human apoA-I using lysine-tolysine chemical cross-linking in conjunction with disulfide
cross-linking achieved using selective cysteine mutations. After
proteolysis, cross-linked peptides were verified by sequencing using tandem mass spectrometry. The resulting structure is
compact with roughly four helical regions, amino acids 44−186, bundled together. C- and N-terminal ends, amino acids 1−43
and 187−243, respectively, are folded such that they lie close to one another. An unusual feature of the molecule is the high
degree of connectivity of lysine40 with six other lysines, lysines that are close, for example, lysine59, to distant lysines, for example,
lysine239, that are at the opposite end of the primary sequence. These results are compared and contrasted with other reported
conformations for lipid-free human apoA-I and an NMR study of mouse apoA-I.
acceptor of lipids from ATP-binding cassette transporter A1, a
process that yields nascent high density lipoproteins. Analysis
of lipidated apoA-I conformation yields a belt or twisted belt in
which two strands of apoA-I lie antiparallel to one another. In
contrast, biophysical studies have suggested that a part of lipidfree apoA-I was arranged in a four-helix bundle. To understand
how lipid-free apoA-I opens from a bundle to a belt while
accepting lipid it was necessary to have a more refined model
for the conformation of lipid-free apoA-I. This study reports
the conformation of lipid-free human apoA-I using lysine-tolysine chemical cross-linking in conjunction with disulfide
cross-linking achieved using selective cysteine mutations. After
proteolysis, cross-linked peptides were verified by sequencing using tandem mass spectrometry. The resulting structure is
compact with roughly four helical regions, amino acids 44−186, bundled together. C- and N-terminal ends, amino acids 1−43
and 187−243, respectively, are folded such that they lie close to one another. An unusual feature of the molecule is the high
degree of connectivity of lysine40 with six other lysines, lysines that are close, for example, lysine59, to distant lysines, for example,
lysine239, that are at the opposite end of the primary sequence. These results are compared and contrasted with other reported
conformations for lipid-free human apoA-I and an NMR study of mouse apoA-I.
การแปล กรุณารอสักครู่..
摘要：载脂蛋白（载脂蛋白A-I）是ATP结合盒转运体A1脂类的主要
受体，一个
过程中产生的新生的高密度脂蛋白。分析
脂apoA-I的构象产生一个带或
这两股apoA-I的扭带到另一个反平行的谎言。在
对比，生物物理研究表明lipidfree apoA-I的一部分被安排在一四螺旋束。了解如何从一个
无脂apoA-I束打开一个带而
接受脂质是需要有一个更重fi内德模型
为无脂apoA-I的这项研究报告的
构象构象的脂质自由人apoA-I的利用赖氨酸tolysine化学交联与2fide
交联结合使用有选择性的半胱氨酸突变的实现。
蛋白水解后的交联的肽fi，验证通过使用串联质谱测序。所得到的结构是
紧凑的大约四个螺旋区域，44个氨基酸−186，捆绑在一起。C和N-末端氨基酸43，1−
−243和187，分别是折叠的，这样他们的谎言接近另一个。分子的一个不同寻常的特点是与其他六个赖氨酸的连通性lysine40
程度高，赖氨酸，是亲密的，例如，lysine59，到遥远的赖氨酸，例如，
lysine239，是在原序列的另一端。这些结果进行了比较与其他报道
构象的脂质自由人apoA-1和小鼠ApoA-I NMR研究对比
受体，一个
过程中产生的新生的高密度脂蛋白。分析
脂apoA-I的构象产生一个带或
这两股apoA-I的扭带到另一个反平行的谎言。在
对比，生物物理研究表明lipidfree apoA-I的一部分被安排在一四螺旋束。了解如何从一个
无脂apoA-I束打开一个带而
接受脂质是需要有一个更重fi内德模型
为无脂apoA-I的这项研究报告的
构象构象的脂质自由人apoA-I的利用赖氨酸tolysine化学交联与2fide
交联结合使用有选择性的半胱氨酸突变的实现。
蛋白水解后的交联的肽fi，验证通过使用串联质谱测序。所得到的结构是
紧凑的大约四个螺旋区域，44个氨基酸−186，捆绑在一起。C和N-末端氨基酸43，1−
−243和187，分别是折叠的，这样他们的谎言接近另一个。分子的一个不同寻常的特点是与其他六个赖氨酸的连通性lysine40
程度高，赖氨酸，是亲密的，例如，lysine59，到遥远的赖氨酸，例如，
lysine239，是在原序列的另一端。这些结果进行了比较与其他报道
构象的脂质自由人apoA-1和小鼠ApoA-I NMR研究对比
การแปล กรุณารอสักครู่..
ภาษาอื่น ๆ
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