메뉴 건너뛰기




Volumn 113, Issue 11, 2016, Pages 2940-2945

Leukocyte integrin αlβ2 headpiece structures: The αi domain, the pocket for the internal ligand, and concerted movements of its loops

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAXBETA2 INTEGRIN; CD18 ANTIGEN; DISULFIDE; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR 1; GLYCAN; GLYCOPROTEIN; INTEGRIN; INTEGRIN ALPHALBETA2; LEUKOCYTE ANTIGEN; MEMBRANE PROTEIN; N GLYCAN; PYROGLUTAMIC ACID; SPECIFICITY DETERMINING LOOP 1; SPECIFICITY DETERMINING LOOP 2; UNCLASSIFIED DRUG; LIGAND; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; PROTEIN BINDING;

EID: 84961828029     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1601379113     Document Type: Article
Times cited : (39)

References (37)
  • 1
    • 84857688656 scopus 로고    scopus 로고
    • Integrin inside-out signaling and the immunological synapse
    • Springer TA, Dustin ML (2012) Integrin inside-out signaling and the immunological synapse. Curr Opin Cell Biol 24(1):107-115.
    • (2012) Curr Opin Cell Biol , vol.24 , Issue.1 , pp. 107-115
    • Springer, T.A.1    Dustin, M.L.2
  • 2
    • 0001894373 scopus 로고
    • Adhesion structure subpanel 5, leukocyte integrins: CD11a, CD11b, CD11c, CD18
    • eds Schlossman SF, et al. (Oxford Univ Press, New York)
    • Petruzzelli L, Luk J, Springer TA (1995) Adhesion structure subpanel 5, leukocyte integrins: CD11a, CD11b, CD11c, CD18. Leucocyte Typing V: White Cell Differentiation Antigens, eds Schlossman SF, et al. (Oxford Univ Press, New York), pp 1581-1585.
    • (1995) Leucocyte Typing V: White Cell Differentiation Antigens , pp. 1581-1585
    • Petruzzelli, L.1    Luk, J.2    Springer, T.A.3
  • 3
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer TA (1990) Adhesion receptors of the immune system. Nature 346(6283):425-434.
    • (1990) Nature , vol.346 , Issue.6283 , pp. 425-434
    • Springer, T.A.1
  • 4
    • 0023083976 scopus 로고
    • Leukocyte adhesion deficiency: An inherited defect in the Mac-1, LFA-1, and p150,95 glycoproteins
    • Anderson DC, Springer TA (1987) Leukocyte adhesion deficiency: An inherited defect in the Mac-1, LFA-1, and p150,95 glycoproteins. Annu Rev Med 38:175-194.
    • (1987) Annu Rev Med , vol.38 , pp. 175-194
    • Anderson, D.C.1    Springer, T.A.2
  • 5
    • 0036578664 scopus 로고    scopus 로고
    • Psoriasis as a model for T-cell-mediated disease: Immunobiologic and clinical effects of treatment with multiple doses of efalizumab, an anti-CD11a antibody
    • Gottlieb AB, et al. (2002) Psoriasis as a model for T-cell-mediated disease: Immunobiologic and clinical effects of treatment with multiple doses of efalizumab, an anti-CD11a antibody. Arch Dermatol 138(5):591-600.
    • (2002) Arch Dermatol , vol.138 , Issue.5 , pp. 591-600
    • Gottlieb, A.B.1
  • 6
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin
    • Qu A, Leahy DJ (1995) Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. Proc Natl Acad Sci USA 92(22):10277-10281.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.22 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 7
    • 0030586822 scopus 로고    scopus 로고
    • The role of the divalent cation in the structure of the i domain from the CD11a/CD18 integrin
    • Qu A, Leahy DJ (1996) The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin. Structure 4(8):931-942.
    • (1996) Structure , vol.4 , Issue.8 , pp. 931-942
    • Qu, A.1    Leahy, D.J.2
  • 8
    • 0037428080 scopus 로고    scopus 로고
    • Structures of the α L i domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
    • Shimaoka M, et al. (2003) Structures of the α L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell 112(1):99-111.
    • (2003) Cell , vol.112 , Issue.1 , pp. 99-111
    • Shimaoka, M.1
  • 9
    • 14744276916 scopus 로고    scopus 로고
    • An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2
    • Song G, et al. (2005) An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2. Proc Natl Acad Sci USA 102(9):3366-3371.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.9 , pp. 3366-3371
    • Song, G.1
  • 10
    • 48349146151 scopus 로고    scopus 로고
    • An unusual allosteric mobility of the C-terminal helix of a highaffinity alphaL integrin i domain variant bound to ICAM-5
    • Zhang H, et al. (2008) An unusual allosteric mobility of the C-terminal helix of a highaffinity alphaL integrin I domain variant bound to ICAM-5. Mol Cell 31(3):432-437.
    • (2008) Mol Cell , vol.31 , Issue.3 , pp. 432-437
    • Zhang, H.1
  • 11
    • 0034602933 scopus 로고    scopus 로고
    • NMR solution structure of the inserted domain of human leukocyte function associated antigen-1
    • Legge GB, et al. (2000) NMR solution structure of the inserted domain of human leukocyte function associated antigen-1. J Mol Biol 295(5):1251-1264.
    • (2000) J Mol Biol , vol.295 , Issue.5 , pp. 1251-1264
    • Legge, G.B.1
  • 12
    • 84928952253 scopus 로고    scopus 로고
    • NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain
    • Leung HT, et al. (2014) NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain. Protein Sci 23(11):1596-1606.
    • (2014) Protein Sci , vol.23 , Issue.11 , pp. 1596-1606
    • Leung, H.T.1
  • 13
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an alphaI domain, complement receptor type 4
    • Xie C, et al. (2010) Structure of an integrin with an alphaI domain, complement receptor type 4. EMBO J 29(3):666-679.
    • (2010) EMBO J , vol.29 , Issue.3 , pp. 666-679
    • Xie, C.1
  • 14
    • 24044494270 scopus 로고    scopus 로고
    • The crystal structure of the plexin-semaphorin-integrin domain/ hybrid domain/I-EGF1 segment from the human integrin β2 subunit at 1.8-A resolution
    • Shi M, et al. (2005) The crystal structure of the plexin-semaphorin-integrin domain/ hybrid domain/I-EGF1 segment from the human integrin β2 subunit at 1.8-A resolution. J Biol Chem 280(34):30586-30593.
    • (2005) J Biol Chem , vol.280 , Issue.34 , pp. 30586-30593
    • Shi, M.1
  • 15
    • 35648936537 scopus 로고    scopus 로고
    • A structural hypothesis for the transition between bent and extended conformations of the leukocyte β2 integrins
    • Shi M, et al. (2007) A structural hypothesis for the transition between bent and extended conformations of the leukocyte β2 integrins. J Biol Chem 282(41):30198-30206.
    • (2007) J Biol Chem , vol.282 , Issue.41 , pp. 30198-30206
    • Shi, M.1
  • 16
    • 84890230123 scopus 로고    scopus 로고
    • An internal ligand-bound, metastable state of a leukocyte integrin, αxβ2
    • Sen M, Yuki K, Springer TA (2013) An internal ligand-bound, metastable state of a leukocyte integrin, αXβ2. J Cell Biol 203(4):629-642.
    • (2013) J Cell Biol , vol.203 , Issue.4 , pp. 629-642
    • Sen, M.1    Yuki, K.2    Springer, T.A.3
  • 17
    • 84868589032 scopus 로고    scopus 로고
    • αvβ3 integrin crystal structures and their functional implications
    • Dong X, et al. (2012) αVβ3 integrin crystal structures and their functional implications. Biochemistry 51(44):8814-8828.
    • (2012) Biochemistry , vol.51 , Issue.44 , pp. 8814-8828
    • Dong, X.1
  • 18
    • 84887069747 scopus 로고    scopus 로고
    • Improved low-resolution crystallographic refinement with Phenix and Rosetta
    • DiMaio F, et al. (2013) Improved low-resolution crystallographic refinement with Phenix and Rosetta. Nat Methods 10(11):1102-1104.
    • (2013) Nat Methods , vol.10 , Issue.11 , pp. 1102-1104
    • DiMaio, F.1
  • 19
    • 84863012638 scopus 로고    scopus 로고
    • Structural specializations of α4β7, an integrin that mediates rolling adhesion
    • Yu Y, et al. (2012) Structural specializations of α4β7, an integrin that mediates rolling adhesion. J Cell Biol 196(1):131-146.
    • (2012) J Cell Biol , vol.196 , Issue.1 , pp. 131-146
    • Yu, Y.1
  • 20
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • Zhu J, et al. (2008) Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol Cell 32(6):849-861.
    • (2008) Mol Cell , vol.32 , Issue.6 , pp. 849-861
    • Zhu, J.1
  • 21
    • 84860273145 scopus 로고    scopus 로고
    • Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptor
    • Nagae M, et al. (2012) Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptor. J Cell Biol 197(1):131-140.
    • (2012) J Cell Biol , vol.197 , Issue.1 , pp. 131-140
    • Nagae, M.1
  • 22
    • 84924179168 scopus 로고    scopus 로고
    • Structural determinants of integrin β-subunit specificity for latent TGF-β
    • Dong X, Hudson NE, Lu C, Springer TA (2014) Structural determinants of integrin β-subunit specificity for latent TGF-β. Nat Struct Mol Biol 21(12):1091-1096.
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.12 , pp. 1091-1096
    • Dong, X.1    Hudson, N.E.2    Lu, C.3    Springer, T.A.4
  • 23
    • 84919363205 scopus 로고    scopus 로고
    • Metal ion and ligand binding of integrin α5β1
    • Xia W, Springer TA (2014) Metal ion and ligand binding of integrin α5β1. Proc Natl Acad Sci USA 111(50):17863-17868.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.50 , pp. 17863-17868
    • Xia, W.1    Springer, T.A.2
  • 24
    • 0023666090 scopus 로고
    • Cloning of the β subunit of the leukocyte adhesion proteins: Homology to an extracellular matrix receptor defines a novel supergene family
    • Kishimoto TK, O'Connor K, Lee A, Roberts TM, Springer TA (1987) Cloning of the β subunit of the leukocyte adhesion proteins: Homology to an extracellular matrix receptor defines a novel supergene family. Cell 48(4):681-690.
    • (1987) Cell , vol.48 , Issue.4 , pp. 681-690
    • Kishimoto, T.K.1    O'Connor, K.2    Lee, A.3    Roberts, T.M.4    Springer, T.A.5
  • 25
    • 82755162374 scopus 로고    scopus 로고
    • The C-terminal αi domain linker as a critical structural element in the conformational activation of αi integrins
    • Weitz-Schmidt G, Schürpf T, Springer TA (2011) The C-terminal αI domain linker as a critical structural element in the conformational activation of αI integrins. J Biol Chem 286(49):42115-42122.
    • (2011) J Biol Chem , vol.286 , Issue.49 , pp. 42115-42122
    • Weitz-Schmidt, G.1    Schürpf, T.2    Springer, T.A.3
  • 26
    • 0142026204 scopus 로고    scopus 로고
    • Therapeutic antagonists and conformational regulation of integrin function
    • Shimaoka M, Springer TA (2003) Therapeutic antagonists and conformational regulation of integrin function. Nat Rev Drug Discov 2(9):703-716.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.9 , pp. 703-716
    • Shimaoka, M.1    Springer, T.A.2
  • 27
    • 84880008208 scopus 로고    scopus 로고
    • Complete integrin headpiece opening in eight steps
    • Zhu J, Zhu J, Springer TA (2013) Complete integrin headpiece opening in eight steps. J Cell Biol 201(7):1053-1068.
    • (2013) J Cell Biol , vol.201 , Issue.7 , pp. 1053-1068
    • Zhu, J.1    Zhu, J.2    Springer, T.A.3
  • 28
    • 0036499161 scopus 로고    scopus 로고
    • The role of the CPNKEKEC sequence in the β2 subunit i domain in regulation of integrin αlβ2 (LFA-1)
    • Kamata T, et al. (2002) The role of the CPNKEKEC sequence in the β2 subunit I domain in regulation of integrin αLβ2 (LFA-1). J Immunol 168(5):2296-2301.
    • (2002) J Immunol , vol.168 , Issue.5 , pp. 2296-2301
    • Kamata, T.1
  • 29
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αvβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong JP, et al. (2002) Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science 296(5565):151-155.
    • (2002) Science , vol.296 , Issue.5565 , pp. 151-155
    • Xiong, J.P.1
  • 30
    • 50249106884 scopus 로고    scopus 로고
    • Structural basis for distinctive recognition of fibrinogen γc peptide by the platelet integrin αiIbβ3
    • Springer TA, Zhu J, Xiao T (2008) Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3. J Cell Biol 182(4):791-800.
    • (2008) J Cell Biol , vol.182 , Issue.4 , pp. 791-800
    • Springer, T.A.1    Zhu, J.2    Xiao, T.3
  • 31
    • 52949142769 scopus 로고    scopus 로고
    • Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs
    • Mi LZ, et al. (2008) Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs. Biochemistry 47(39): 10314-10323.
    • (2008) Biochemistry , vol.47 , Issue.39 , pp. 10314-10323
    • Mi, L.Z.1
  • 32
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG (2002) Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci USA 99(21):13419-13424.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 33
    • 0038786304 scopus 로고    scopus 로고
    • F, crystallography of biological macromolecules
    • eds Rossmann MG, Arnold E (Kluwer Academic Publishers, Dordrecht, The Netherlands)
    • Kabsch W(2001) F, crystallography of biological macromolecules. International Tables for Crystallography, eds Rossmann MG, Arnold E (Kluwer Academic Publishers, Dordrecht, The Netherlands), pp 730-734.
    • (2001) International Tables for Crystallography , pp. 730-734
    • Kabsch, W.1
  • 34
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 35
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Pt 1
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. (2007) MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35(Web Server issue):W375-W383.
    • (2007) Nucleic Acids Res , vol.35 , Issue.WEB SERVER ISSUE , pp. W375-W383
    • Davis, I.W.1
  • 37
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus PA, Diederichs K (2012) Linking crystallographic model and data quality. Science 336(6084):1030-1033.
    • (2012) Science , vol.336 , Issue.6084 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.