Project 3/Struct. of the CDB3:ankyrin:protein 4.2 complex in erythrocytes by EPR
项目 3/结构。
基本信息
- 批准号:7449168
- 负责人:
- 金额:$ 19.52万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:2008
- 资助国家:美国
- 起止时间:2008-05-01 至 2013-04-30
- 项目状态:已结题
- 来源:
- 关键词:ActinsAdaptor Signaling ProteinAffinityAldehyde-LyasesAmino AcidsAnion Exchangers (Proteins)Ankyrin RepeatAnkyrinsArchitectureBindingBinding ProteinsBlood CirculationBlood capillariesCardiovascular systemCell ShapeCell SizeCell membraneCellsClassComplexConditionCytoplasmic TailDNA Sequence RearrangementDataDefectDiseaseDockingErythrocyte MembraneErythrocytesExhibitsFamilyFluorescenceFructosediphosphate AldolaseGlycophorin CGoalsHemoglobinHemolysisHemolytic AnemiaHereditary SpherocytosisHomology ModelingHumanIntegral Membrane ProteinKnowledgeLabelLaboratoriesLeadLengthLipid BilayersLiteratureMechanicsMembraneMembrane ProteinsMethodsMicrocirculationModelingMolecularPeripheralPhenotypePhysiologic pulsePoint MutationPositioning AttributePropertyProteinsPulse takingRangeRelative (related person)ReportingResolutionShapesSideSiteSkeletonSpectrinSpin LabelsStructural ModelsStructureSurfaceTestingWorkadapter proteinband 3 protein Tuscaloosabasecapillarydimerhuman SYK proteininsightmolecular dynamicsmolecular modelingprotein 4.1protein protein interactionshear stress
项目摘要
Human erythrocytes exhibit an unusual biconcave disc shape together with remarkable stability and
deformability, all of which are necessary for their survival in the circulatory system. It is now well established
that the unusual cell shape and membrane mechanical properties are due in large part to the presence of an
extensive membrane skeleton, composed primarily of the proteins spectrin and actin, that lines the inner
membrane surface and to specific bridging interactions between this membrane skeleton and intrinsic
membrane proteins in the lipid bilayer. The spectrin-actin skeleton associates with the membrane bilayer via
two types of contacts, one involving short actin protofilaments and protein 4.1 interacting with the cytoplasmic
domain of glycophorin C, and the second involving the bridging protein ankyrinR and protein 4.2 interacting
with the cytoplasmic domain of the anion exchange protein (AE1). This project seeks to characterize the
structure of the complex of proteins that forms this second class of bridging interactions in human erythrocytes.
This focus is dictated by the knowledge that alterations in this second class of interactions results in spherical
erythrocytes with decreased cell size and increased fragility, a condition known clinically as hereditary
spherocytosis (HS). HS is a spectrum of diseases, occurring in one family out of 2,000 to 3,000, that present
clinically as varying degrees of hemolytic anemia resulting from hemolysis of the spherical erythrocytes when
they traverse the microcirculation. Recent data have indicated that 15-20% of HS cases are attributable to AE1
defects and ~50% of HS cases result from ankyrin defects (4). A reduction in protein 4.2 binding to the
membrane is also a common finding (5).
Studies over the past three decades have led to the definition of the intrinsic and peripheral membrane
proteins that assemble to stabilize the erythrocyte membrane (reviewed in (6,7)). A central player in the
assembly of these proteins is the cytoplasmic domain of AE1 (also known as band 3). The cytoplasmic domain
of band 3 (cdb3) has been hypothesized to serve as an organizing center for binding ankyrinR (8) and protein
4.2 (9) as well as other cytosolic proteins including GAPDH (10,11), aldolase (12), phosphofructokinase (13),
hemoglobin (14), hemichromes (15), and p72syk (16). Figure 1 shows a schematic diagram of some of the key
protein-protein interactions that have been elucidated.
人红细胞表现出不寻常的双凹盘状,具有显著的稳定性和稳定性
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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ALBERT H BETH其他文献
ALBERT H BETH的其他文献
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{{ truncateString('ALBERT H BETH', 18)}}的其他基金
STRUCTURE OF THE CDB3:ANKYRINR COMPLEX IN ERYTHROCYTES BY EPR
通过 EPR 分析红细胞中 CDB3: 锚蛋白复合物的结构
- 批准号:
8364096 - 财政年份:2011
- 资助金额:
$ 19.52万 - 项目类别:
Vanderbilt Summer Research Experience for Undergraduates
范德比尔特大学本科生暑期研究经历
- 批准号:
6886759 - 财政年份:2003
- 资助金额:
$ 19.52万 - 项目类别:
Vanderbilt Summer Research Experience for Undergraduates
范德比尔特大学本科生暑期研究经历
- 批准号:
7057791 - 财政年份:2003
- 资助金额:
$ 19.52万 - 项目类别:
Vanderbilt Summer Research Experience for Undergraduates
范德比尔特大学本科生暑期研究经历
- 批准号:
6568224 - 财政年份:2003
- 资助金额:
$ 19.52万 - 项目类别:
Vanderbilt Summer Research Experience for Undergraduates
范德比尔特大学本科生暑期研究经历
- 批准号:
6740238 - 财政年份:2003
- 资助金额:
$ 19.52万 - 项目类别:
Spectroscopic Studies of EGF-Receptor Interactions
EGF-受体相互作用的光谱研究
- 批准号:
6905530 - 财政年份:1997
- 资助金额:
$ 19.52万 - 项目类别: