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Volumn 31, Issue 3, 2008, Pages 432-437

An Unusual Allosteric Mobility of the C-Terminal Helix of a High-Affinity αL Integrin I Domain Variant Bound to ICAM-5

Author keywords

PROTEIN; SIGNALING

Indexed keywords

ALPHA INTEGRIN; CELL ADHESION MOLECULE; INTERCELLULAR ADHESION MOLECULE 5; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1;

EID: 48349146151     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2008.06.022     Document Type: Article
Times cited : (31)

References (26)
  • 1
    • 0030916713 scopus 로고    scopus 로고
    • Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface
    • Casasnovas J.M., Springer T.A., Liu J.H., Harrison S.C., and Wang J.-H. Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface. Nature 387 (1997) 312-315
    • (1997) Nature , vol.387 , pp. 312-315
    • Casasnovas, J.M.1    Springer, T.A.2    Liu, J.H.3    Harrison, S.C.4    Wang, J.-H.5
  • 2
    • 0032516060 scopus 로고    scopus 로고
    • A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1
    • Casasnovas J.M., Stehle T., Liu J.-H., Wang J.-H., and Springer T.A. A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1. Proc. Natl. Acad. Sci. USA 95 (1998) 4134-4139
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4134-4139
    • Casasnovas, J.M.1    Stehle, T.2    Liu, J.-H.3    Wang, J.-H.4    Springer, T.A.5
  • 3
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50 (1994) 760-763
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 6
    • 0030854195 scopus 로고    scopus 로고
    • Leukocyte adhesion: CD11/CD18 integrins and intercellular adhesion molecules
    • Gahmberg C.G. Leukocyte adhesion: CD11/CD18 integrins and intercellular adhesion molecules. Curr. Opin. Cell Biol. 9 (1997) 643-650
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 643-650
    • Gahmberg, C.G.1
  • 7
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 110 (2002) 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 9
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee J.O., Rieu P., Arnaout M.A., and Liddington R. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80 (1995) 631-638
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 11
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo B.H., Carman C.V., and Springer T.A. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25 (2007) 619-647
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 12
    • 0031022515 scopus 로고    scopus 로고
    • cDNA cloning and chromosomal localization of the human telencephalin and its distinctive interaction with lymphocyte function-associated antigen-1
    • Mizuno T., Yoshihara Y., Inazawa J., Kagamiyama H., and Mori K. cDNA cloning and chromosomal localization of the human telencephalin and its distinctive interaction with lymphocyte function-associated antigen-1. J. Biol. Chem. 272 (1997) 1156-1163
    • (1997) J. Biol. Chem. , vol.272 , pp. 1156-1163
    • Mizuno, T.1    Yoshihara, Y.2    Inazawa, J.3    Kagamiyama, H.4    Mori, K.5
  • 15
    • 0025287826 scopus 로고
    • Mammalian telencephalic neurons express a segment-specific membrane glycoprotein, telencephalin
    • Oka S., Mori K., and Watanabe Y. Mammalian telencephalic neurons express a segment-specific membrane glycoprotein, telencephalin. Neuroscience 35 (1990) 93-103
    • (1990) Neuroscience , vol.35 , pp. 93-103
    • Oka, S.1    Mori, K.2    Watanabe, Y.3
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carte Jr. C.W., and Sweet R.M. (Eds), Academic Press, San Diego, London, Boston, New York, Sydney, Tokyo, Toronto
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carte Jr. C.W., and Sweet R.M. (Eds). Macromolecular Crystallography (1997), Academic Press, San Diego, London, Boston, New York, Sydney, Tokyo, Toronto 307-326
    • (1997) Macromolecular Crystallography , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin
    • Qu A., and Leahy D.J. Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. Proc. Natl. Acad. Sci. USA 92 (1995) 10277-10281
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 18
    • 0035932996 scopus 로고    scopus 로고
    • Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin αL I domains with high affinity and antagonist activity in vivo
    • Shimaoka M., Lu C., Palframan R., von Andrian U.H., Takagi J., and Springer T.A. Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin αL I domains with high affinity and antagonist activity in vivo. Proc. Natl. Acad. Sci. USA 98 (2001) 6009-6014
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6009-6014
    • Shimaoka, M.1    Lu, C.2    Palframan, R.3    von Andrian, U.H.4    Takagi, J.5    Springer, T.A.6
  • 20
    • 0037428080 scopus 로고    scopus 로고
    • Structures of the alphaL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
    • Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A., Zhang R., Joachimiak A., Takagi J., et al. Structures of the alphaL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell 112 (2003) 99-111
    • (2003) Cell , vol.112 , pp. 99-111
    • Shimaoka, M.1    Xiao, T.2    Liu, J.H.3    Yang, Y.4    Dong, Y.5    Jun, C.D.6    McCormack, A.7    Zhang, R.8    Joachimiak, A.9    Takagi, J.10
  • 21
    • 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., Yang Y., Liu J.H., Casasnovas J.M., Shimaoka M., Springer T.A., and Wang J.H. 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 (2005) 3366-3371
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3366-3371
    • Song, G.1    Yang, Y.2    Liu, J.H.3    Casasnovas, J.M.4    Shimaoka, M.5    Springer, T.A.6    Wang, J.H.7
  • 22
    • 14744273494 scopus 로고    scopus 로고
    • The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion
    • Springer T.A., and Wang J.H. The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion. Adv. Protein Chem. 68 (2004) 29-63
    • (2004) Adv. Protein Chem. , vol.68 , pp. 29-63
    • Springer, T.A.1    Wang, J.H.2
  • 23
    • 0031567984 scopus 로고    scopus 로고
    • The neuronal glycoprotein telencephalin is a cellular ligand for the CD11a/CD18 leukocyte integrin
    • Tian L., Yoshihara Y., Mizuno T., Mori K., and Gahmberg C.G. The neuronal glycoprotein telencephalin is a cellular ligand for the CD11a/CD18 leukocyte integrin. J. Immunol. 158 (1997) 928-936
    • (1997) J. Immunol. , vol.158 , pp. 928-936
    • Tian, L.1    Yoshihara, Y.2    Mizuno, T.3    Mori, K.4    Gahmberg, C.G.5
  • 25
    • 0036496114 scopus 로고    scopus 로고
    • Protein recognition by cell surface receptors: physiological receptors versus virus interactions
    • Wang J. Protein recognition by cell surface receptors: physiological receptors versus virus interactions. Trends Biochem. Sci. 27 (2002) 122-126
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 122-126
    • Wang, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.