메뉴 건너뛰기




Volumn 111, Issue 24, 2014, Pages 8877-8882

Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα

Author keywords

Immune regulation; O glycosylated protein; Paired receptor; X ray crystallography

Indexed keywords

GLYCAN; GLYCOSYLATED PROTEIN; LIGAND; MUCIN; PAIRED IMMUNOGLOBULIN LIKE TYPE 2 RECEPTOR ALPHA; PROLINE; RECEPTOR; UNCLASSIFIED DRUG;

EID: 84902593774     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1324105111     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 40749160803 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation and its potential use in drug and vaccine development
    • DOI 10.1016/j.bbagen.2007.09.010, PII S0304416507002164
    • Tarp MA, Clausen H (2008) Mucin-type O-glycosylation and its potential use in drug and vaccine development. Biochim Biophys Acta 1780(3):546-563. (Pubitemid 351381249)
    • (2008) Biochimica et Biophysica Acta - General Subjects , vol.1780 , Issue.3 , pp. 546-563
    • Tarp, M.A.1    Clausen, H.2
  • 2
    • 0034613151 scopus 로고    scopus 로고
    • Immune inhibitory receptors
    • Ravetch JV, Lanier LL (2000) Immune inhibitory receptors. Science 290(5489):84-89.
    • (2000) Science , vol.290 , Issue.5489 , pp. 84-89
    • Ravetch, J.V.1    Lanier, L.L.2
  • 3
    • 49249103754 scopus 로고    scopus 로고
    • Immunoreceptor tyrosine-based inhibition motifs: A quest in the past and future
    • Daëron M, Jaeger S, Du Pasquier L, Vivier E (2008) Immunoreceptor tyrosine-based inhibition motifs: A quest in the past and future. Immunol Rev 224:11-43.
    • (2008) Immunol Rev , vol.224 , pp. 11-43
    • Daëron, M.1    Jaeger, S.2    Du Pasquier, L.3    Vivier, E.4
  • 4
    • 84875883066 scopus 로고    scopus 로고
    • Molecular recognition of paired receptors in the immune system
    • Kuroki K, Furukawa A, Maenaka K (2012) Molecular recognition of paired receptors in the immune system. Front Microbiol 3:429.
    • (2012) Front Microbiol , vol.3 , pp. 429
    • Kuroki, K.1    Furukawa, A.2    Maenaka, K.3
  • 5
    • 0035366156 scopus 로고    scopus 로고
    • Face off - The interplay between activating and inhibitory immune receptors
    • Lanier LL (2001) Face off - the interplay between activating and inhibitory immune receptors. Curr Opin Immunol 13(3):326-331.
    • (2001) Curr Opin Immunol , vol.13 , Issue.3 , pp. 326-331
    • Lanier, L.L.1
  • 6
    • 1242343695 scopus 로고    scopus 로고
    • Activation of Natural Killer Cells and Dendritic Cells upon Recognition of a Novel CD99-like Ligand by Paired Immunoglobulin-like Type 2 Receptor
    • DOI 10.1084/jem.20031885
    • Shiratori I, Ogasawara K, Saito T, Lanier LL, Arase H (2004) Activation of natural killer cells and dendritic cells upon recognition of a novel CD99-like ligand by paired immunoglobulin-like type 2 receptor. J Exp Med 199(4):525-533. (Pubitemid 38233836)
    • (2004) Journal of Experimental Medicine , vol.199 , Issue.4 , pp. 525-533
    • Shiratori, I.1    Ogasawara, K.2    Saito, T.3    Lanier, L.L.4    Arase, H.5
  • 8
    • 84860875016 scopus 로고    scopus 로고
    • Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands
    • Sun Y, et al. (2012) Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands. J Biol Chem 287(19):15837-15850.
    • (2012) J Biol Chem , vol.287 , Issue.19 , pp. 15837-15850
    • Sun, Y.1
  • 9
    • 77349102446 scopus 로고    scopus 로고
    • Modulation of paired immunoglobulin-like type 2 receptor signaling alters the host response to Staphylococcus aureus-induced pneumonia
    • Banerjee A, et al. (2010) Modulation of paired immunoglobulin-like type 2 receptor signaling alters the host response to Staphylococcus aureus-induced pneumonia. Infect Immun 78(3):1353-1363.
    • (2010) Infect Immun , vol.78 , Issue.3 , pp. 1353-1363
    • Banerjee, A.1
  • 10
    • 84871239583 scopus 로고    scopus 로고
    • Neutrophil infiltration during inflammation is regulated by PILRα via modulation of integrin activation
    • Wang J, Shiratori I, Uehori J, Ikawa M, Arase H (2013) Neutrophil infiltration during inflammation is regulated by PILRα via modulation of integrin activation. Nat Immunol 14(1):34-40.
    • (2013) Nat Immunol , vol.14 , Issue.1 , pp. 34-40
    • Wang, J.1    Shiratori, I.2    Uehori, J.3    Ikawa, M.4    Arase, H.5
  • 11
    • 44049092612 scopus 로고    scopus 로고
    • Biophysical characterization of O-glycosylated CD99 recognition by paired Ig-like type 2 receptors
    • Tabata S, et al. (2008) Biophysical characterization of O-glycosylated CD99 recognition by paired Ig-like type 2 receptors. J Biol Chem 283(14):8893-8901.
    • (2008) J Biol Chem , vol.283 , Issue.14 , pp. 8893-8901
    • Tabata, S.1
  • 12
    • 0037123607 scopus 로고    scopus 로고
    • Direct recognition of cytomegalovirus by activating and inhibitory NK cell receptors
    • DOI 10.1126/science.1070884
    • Arase H, Mocarski ES, Campbell AE, Hill AB, Lanier LL (2002) Direct recognition of cytomegalovirus by activating and inhibitory NK cell receptors. Science 296(5571):1323-1326. (Pubitemid 34522789)
    • (2002) Science , vol.296 , Issue.5571 , pp. 1323-1326
    • Arase, H.1    Mocarski, E.S.2    Campbell, A.E.3    Hill, A.B.4    Lanier, L.L.5
  • 13
    • 0030768392 scopus 로고    scopus 로고
    • A novel immunoglobulin superfamily receptor for cellular and viral MHC class I molecules
    • DOI 10.1016/S1074-7613(00)80529-4
    • Cosman D, et al. (1997) A novel immunoglobulin superfamily receptor for cellular and viral MHC class I molecules. Immunity 7(2):273-282. (Pubitemid 27392018)
    • (1997) Immunity , vol.7 , Issue.2 , pp. 273-282
    • Cosman, D.1    Fanger, N.2    Borges, L.3    Kubin, M.4    Chin, W.5    Peterson, L.6    Hsu, M.-L.7
  • 15
    • 77955272566 scopus 로고    scopus 로고
    • A novel KIR-associated function: Evidence that CpG DNA uptake and shuttling to early endosomes is mediated by KIR3DL2
    • Sivori S, et al. (2010) A novel KIR-associated function: Evidence that CpG DNA uptake and shuttling to early endosomes is mediated by KIR3DL2. Blood 116(10):1637-1647.
    • (2010) Blood , vol.116 , Issue.10 , pp. 1637-1647
    • Sivori, S.1
  • 17
    • 72849125119 scopus 로고    scopus 로고
    • Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor α depends on specific sialylated O-linked glycans on gB
    • Wang J, et al. (2009) Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor α depends on specific sialylated O-linked glycans on gB. J Virol 83(24):13042-13045.
    • (2009) J Virol , vol.83 , Issue.24 , pp. 13042-13045
    • Wang, J.1
  • 18
    • 40749122107 scopus 로고    scopus 로고
    • An essential role of sialylated O-linked sugar chains in the recognition of mouse CD99 by paired Ig-like type 2 receptor (PILR)
    • Wang J, Shiratori I, Satoh T, Lanier LL, Arase H (2008) An essential role of sialylated O-linked sugar chains in the recognition of mouse CD99 by paired Ig-like type 2 receptor (PILR). J Immunol 180(3):1686-1693.
    • (2008) J Immunol , vol.180 , Issue.3 , pp. 1686-1693
    • Wang, J.1    Shiratori, I.2    Satoh, T.3    Lanier, L.L.4    Arase, H.5
  • 20
    • 37549036760 scopus 로고    scopus 로고
    • Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα)
    • Tabata S, et al. (2008) Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα). Acta Crystallogr Sect F Struct Biol Cryst Commun 64(Pt 1):44-46.
    • (2008) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.64 , Issue.PART 1 , pp. 44-46
    • Tabata, S.1
  • 21
    • 0032037915 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 a resolution
    • May AP, Robinson RC, Vinson M, Crocker PR, Jones EY (1998) Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution. Mol Cell 1(5):719-728. (Pubitemid 128379249)
    • (1998) Molecular Cell , vol.1 , Issue.5 , pp. 719-728
    • May, A.P.1    Robinson, R.C.2    Vinson, M.3    Crocker, P.R.4    Jones, E.Y.5
  • 22
    • 34247565506 scopus 로고    scopus 로고
    • Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins
    • Varki A (2007) Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins. Nature 446(7139):1023-1029.
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1023-1029
    • Varki, A.1
  • 23
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • DOI 10.1038/nri2056, PII NRI2056
    • Crocker PR, Paulson JC, Varki A (2007) Siglecs and their roles in the immune system. Nat Rev Immunol 7(4):255-266. (Pubitemid 46480955)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.4 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 24
    • 34247107234 scopus 로고    scopus 로고
    • Sialic acid on herpes simplex virus type 1 envelope glycoproteins is required for efficient infection of cells
    • DOI 10.1128/JVI.02250-06
    • Teuton JR, Brandt CR (2007) Sialic acid on herpes simplex virus type 1 envelope glycoproteins is required for efficient infection of cells. J Virol 81(8):3731-3739. (Pubitemid 46586870)
    • (2007) Journal of Virology , vol.81 , Issue.8 , pp. 3731-3739
    • Teuton, J.R.1    Brandt, C.R.2
  • 25
    • 77956621608 scopus 로고    scopus 로고
    • The Ig-like v-type domain of paired Ig-like type 2 receptor alpha is critical for herpes simplex virus type 1-mediated membrane fusion
    • Fan Q, Longnecker R (2010) The Ig-like v-type domain of paired Ig-like type 2 receptor alpha is critical for herpes simplex virus type 1-mediated membrane fusion. J Virol 84(17):8664-8672.
    • (2010) J Virol , vol.84 , Issue.17 , pp. 8664-8672
    • Fan, Q.1    Longnecker, R.2
  • 26
    • 0022555847 scopus 로고
    • Carbohydrate-binding proteins: Tertiary structures and protein-sugar interactions
    • Quiocho FA (1986) Carbohydrate-binding proteins: Tertiary structures and protein-sugar interactions. Annu Rev Biochem 55:287-315.
    • (1986) Annu Rev Biochem , vol.55 , pp. 287-315
    • Quiocho, F.A.1
  • 27
    • 0024189319 scopus 로고
    • Molecular features and basic understanding of protein-carbohydrate interactions: The arabinose-binding protein-sugar complex
    • Quiocho FA (1988) Molecular features and basic understanding of protein-carbohydrate interactions: The arabinose-binding protein-sugar complex. Curr Top Microbiol Immunol 139:135-148.
    • (1988) Curr Top Microbiol Immunol , vol.139 , pp. 135-148
    • Quiocho, F.A.1
  • 28
    • 77952559114 scopus 로고    scopus 로고
    • Effect of glycosylation on cis/trans isomerization of prolines in IgA1-hinge peptide
    • Narimatsu Y, et al. (2010) Effect of glycosylation on cis/trans isomerization of prolines in IgA1-hinge peptide. J Am Chem Soc 132(16):5548-5549.
    • (2010) J Am Chem Soc , vol.132 , Issue.16 , pp. 5548-5549
    • Narimatsu, Y.1
  • 29
    • 0034721650 scopus 로고    scopus 로고
    • Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1
    • Somers WS, Tang J, Shaw GD, Camphausen RT (2000) Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1. Cell 103(3):467-479.
    • (2000) Cell , vol.103 , Issue.3 , pp. 467-479
    • Somers, W.S.1    Tang, J.2    Shaw, G.D.3    Camphausen, R.T.4
  • 32
    • 0035849323 scopus 로고    scopus 로고
    • Herpes simplex virus infections
    • DOI 10.1016/S0140-6736(00)04638-9
    • Whitley RJ, Roizman B (2001) Herpes simplex virus infections. Lancet 357(9267):1513-1518. (Pubitemid 32488876)
    • (2001) Lancet , vol.357 , Issue.9267 , pp. 1513-1518
    • Whitley, R.J.1    Roizman, B.2
  • 33
    • 66149115121 scopus 로고    scopus 로고
    • Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor α
    • Arii J, et al. (2009) Entry of herpes simplex virus 1 and other alphaherpesviruses via the paired immunoglobulin-like type 2 receptor α. J Virol 83(9):4520-4527.
    • (2009) J Virol , vol.83 , Issue.9 , pp. 4520-4527
    • Arii, J.1
  • 34
    • 77957190681 scopus 로고    scopus 로고
    • A single-amino-acid substitution in herpes simplex virus 1 envelope glycoprotein B at a site required for binding to the paired immunoglobulin-like type 2 receptor alpha (PILRalpha) abrogates PILRα-dependent viral entry and reduces pathogenesis
    • Arii J, et al. (2010) A single-amino-acid substitution in herpes simplex virus 1 envelope glycoprotein B at a site required for binding to the paired immunoglobulin-like type 2 receptor alpha (PILRalpha) abrogates PILRα-dependent viral entry and reduces pathogenesis. J Virol 84(20):10773-10783.
    • (2010) J Virol , vol.84 , Issue.20 , pp. 10773-10783
    • Arii, J.1
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in Oscillation mode. Methods Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein C, Blanc E, Roversi P, Bricogne G (2007) Automated structure solution with autoSHARP. Methods Mol Biol 364:215-230. (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50(Pt 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763
  • 39
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System (CNS), a new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography & NMR System (CNS), a new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54(Pt 5):905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , Issue.PART 5 , pp. 905-921
    • Brunger, A.T.1
  • 40
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Cα geometry: φ,ψ and Cβ deviation
    • Lovell SC, et al. (2003) Structure validation by Cα geometry: φ,ψ and Cβ deviation. Proteins 50(3):437-450.
    • (2003) Proteins , vol.50 , Issue.3 , pp. 437-450
    • Lovell, S.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.