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Title:
Conformational Stability Analyses of Alpha Subunit I Domain of LFA-1 and Mac-1
Author: Mao DB(毛德斌); Lv SQ(吕守芹); Li N(李宁); Zhang Y(章燕); Long M(龙勉)
Source: PLOS One
Issued Date: 2011
Volume: 6, Issue:8, Pages:e24188
Abstract: beta(2) integrin of lymphocyte function-associated antigen-1 (LFA-1) or macrophage-1 antigen (Mac-1) binds to their common ligand of intercellular adhesion molecule-1 (ICAM-1) and mediates leukocyte-endothelial cell (EC) adhesions in inflammation cascade. Although the two integrins are known to have distinct functions, the corresponding micro-structural bases remain unclear. Here (steered-)molecular dynamics simulations were employed to elucidate the conformational stability of a subunit I domains of LFA-1 and Mac-1 in different affinity states and relevant I domain-ICAM-1 interaction features. Compared with low affinity (LA) Mac-1, the LA LFA-1 I domain was unstable in the presence or absence of ICAM-1 ligand, stemming from diverse orientations of its alpha(7)-helix with different motifs of zipper-like hydrophobic junction between alpha(1)- and alpha(7)-helices. Meanwhile, spontaneous transition of LFA-1 I domain from LA state to intermediate affinity (IA) state was first visualized. All the LA, IA, and high affinity (HA) states of LFA-1 I domain and HA Mac-1 I domain were able to bind to ICAM-1 ligand effectively, while LA Mac-1 I domain was unfavorable for binding ligand presumably due to the specific orientation of S144 side-chain that capped the MIDAS ion. These results furthered our understanding in correlating the structural bases with their functions of LFA-1 and Mac-1 integrins from the viewpoint of I domain conformational stability and of the characteristics of I domain-ICAM-1 interactions.
Keyword: A-Domain ; Molecular-Dynamics ; Structural Basis ; Integrin Activation ; Crystal-Structure ; Cell-Adhesion ; T-Cell ; Neutrophils ; Affinity ; Migration
Language: 英语
Indexed Type: SCI
Corresponding Author: Mao, DB (reprint author), Chinese Acad Sci, Inst Mech, Key Lab Micrograv, Beijing 100080, Peoples R China
Correspondent Email: lsq@imech.ac.cn; mlong@imech.ac.cn
DOI: 10.1371/journal.pone.0024188
Related URLs: 查看原文
DOC Type: Article
WOS Subject: Multidisciplinary Sciences
WOS Subject Extended: Science & Technology - Other Topics
WOS Keyword Plus: A-DOMAIN ; MOLECULAR-DYNAMICS ; STRUCTURAL BASIS ; INTEGRIN ACTIVATION ; CRYSTAL-STRUCTURE ; CELL-ADHESION ; T-CELL ; NEUTROPHILS ; AFFINITY ; MIGRATION
WOS ID: WOS:000294680800064
ISSN: 1932-6203
Rank: [Mao, Debin; Lu, Shouqin; Li, Ning; Zhang, Yan; Long, Mian] Chinese Acad Sci, Inst Mech, Key Lab Micrograv, Beijing 100080, Peoples R China; [Mao, Debin; Lu, Shouqin; Li, Ning; Zhang, Yan; Long, Mian] Chinese Acad Sci, Inst Mech, Natl Micrograv Lab, Beijing 100080, Peoples R China; [Mao, Debin; Lu, Shouqin; Li, Ning; Zhang, Yan; Long, Mian] Chinese Acad Sci, Inst Mech, Ctr Biomech & Bioengn, Beijing 100080, Peoples R China
Subject: Life Sciences & Biomedicine - Other Topics
Department: NML分子-细胞生物力学与空间生命科学
Classification: 二类/Q1
Citation statistics:
Content Type: 期刊论文
URI: http://dspace.imech.ac.cn/handle/311007/45079
Appears in Collections:国家微重力实验室_期刊论文

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Recommended Citation:
Mao DB,Lv SQ,Li N,et al. Conformational Stability Analyses of Alpha Subunit I Domain of LFA-1 and Mac-1[J]. PLOS One,2011-01-01,6(8):e24188.
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