메뉴 건너뛰기




Volumn 52, Issue 3, 2003, Pages 466-477

Comparative analysis of structural properties of the C-type-lectin-like domain (CTLD)

Author keywords

C type lectin; Domain stability; Fold evolution; Hydrophobic core; Structurally conserved residues

Indexed keywords

AEROLYSIN; ASIALOGLYCOPROTEIN RECEPTOR; BINDING PROTEIN; BLOOD CLOTTING FACTOR 10; BOTROCETIN; CD69 ANTIGEN; CD94 ANTIGEN; ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; FISH PROTEIN; GLYCOPROTEIN; INTIMIN; INVASIN; LITHOSTATHINE; LUNG SURFACTANT; MAJOR BASIC PROTEIN; MANNOSE BINDING PROTEIN; MANNOSE RECEPTOR; PADGEM PROTEIN; PERTUSSIS TOXIN; PROTOZOAL PROTEIN; SNAKE VENOM; SURFACTANT PROTEIN D; TETRANECTIN;

EID: 0041671087     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10626     Document Type: Article
Times cited : (105)

References (57)
  • 1
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem 1988;263:9557-9560.
    • (1988) J Biol Chem , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 2
    • 0027359136 scopus 로고
    • Evolution of Ca(2+)-dependent animal lectins
    • Drickamer K. Evolution of Ca(2+)-dependent animal lectins. Prog Nucleic Acid Res Mol Biol 1993;45:207-232.
    • (1993) Prog Nucleic Acid Res Mol Biol , vol.45 , pp. 207-232
    • Drickamer, K.1
  • 3
    • 0032860314 scopus 로고    scopus 로고
    • C-type lectin-like domains
    • Drickamer K. C-type lectin-like domains. Curr Opin Struct Biol 1999;9:585-590.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 585-590
    • Drickamer, K.1
  • 4
    • 0026342025 scopus 로고
    • Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing
    • Weis WI, Kahn R, Fourme R, Drickamer K, Hendrickson WA. Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science 1991;254:1608-1615.
    • (1991) Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3    Drickamer, K.4    Hendrickson, W.A.5
  • 5
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis WI, Drickamer K, Hendrickson WA. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 1992;360:127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 6
    • 0030572693 scopus 로고    scopus 로고
    • Solution structure of the link module: A hyaluronan-binding domain involved in extracellular matrix stability and cell migration
    • Kohda D, Morton CJ, Parkar AA, Hatanaka H, Inagaki FM, Campbell ID, Day AJ. Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration. Cell 1996;86:767-775.
    • (1996) Cell , vol.86 , pp. 767-775
    • Kohda, D.1    Morton, C.J.2    Parkar, A.A.3    Hatanaka, H.4    Inagaki, F.M.5    Campbell, I.D.6    Day, A.J.7
  • 7
    • 0030591452 scopus 로고    scopus 로고
    • The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily
    • Brissett NC, Perkins SJ. The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily. FEBS Lett 1996;388:211-216.
    • (1996) FEBS Lett , vol.388 , pp. 211-216
    • Brissett, N.C.1    Perkins, S.J.2
  • 10
    • 0033536633 scopus 로고    scopus 로고
    • Crystal structure of invasin: A bacterial integrin-binding protein
    • Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ. Crystal structure of invasin: A bacterial integrin-binding protein. Science 1999;286:291-295.
    • (1999) Science , vol.286 , pp. 291-295
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.J.4
  • 11
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 12
    • 0032536859 scopus 로고    scopus 로고
    • Crystal structure of the angiogenesis inhibitor endostatin at 1.5 Å resolution
    • Hohenester E, Sasaki T, Olsen BR, Timpl R. Crystal structure of the angiogenesis inhibitor endostatin at 1.5 Å resolution. EMBO J 1998;17:1656-1664.
    • (1998) EMBO J , vol.17 , pp. 1656-1664
    • Hohenester, E.1    Sasaki, T.2    Olsen, B.R.3    Timpl, R.4
  • 13
    • 0030979409 scopus 로고    scopus 로고
    • Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains
    • Mizuno H, Fujimoto Z, Koizumi M, Kano H, Atoda H, Morita T. Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains. Nat Struct Biol 1997;4:438-441.
    • (1997) Nat Struct Biol , vol.4 , pp. 438-441
    • Mizuno, H.1    Fujimoto, Z.2    Koizumi, M.3    Kano, H.4    Atoda, H.5    Morita, T.6
  • 14
  • 15
    • 0035912739 scopus 로고    scopus 로고
    • Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X
    • Mizuno H, Fujimoto Z, Atoda H, Morita T. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc Natl Acad Sci U S A 2001;98:7230-7234.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 7230-7234
    • Mizuno, H.1    Fujimoto, Z.2    Atoda, H.3    Morita, T.4
  • 17
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu Y, Eisenberg D. 3D domain swapping: as domains continue to swap. Protein Sci 2002;11:1285-1299.
    • (2002) Protein Sci , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 18
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis WI, Drickamer K. Structural basis of lectin-carbohydrate recognition. Annu Rev Biochem 1996;65:441-473.
    • (1996) Annu Rev Biochem , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 19
    • 0036214286 scopus 로고    scopus 로고
    • Structure and function of natural killer cell receptors: Multiple molecular solutions to self, nonself discrimination
    • Natarajan K, Dimasi N, Wang J, Mariuzza RA, Margulies DH. Structure and function of natural killer cell receptors: multiple molecular solutions to self, nonself discrimination. Annu Rev Immunol 2002;20:853-885.
    • (2002) Annu Rev Immunol , vol.20 , pp. 853-885
    • Natarajan, K.1    Dimasi, N.2    Wang, J.3    Mariuzza, R.A.4    Margulies, D.H.5
  • 20
    • 0032549028 scopus 로고    scopus 로고
    • Analysis of chimeric proteins identifies the regions in the carbohydrate recognition domains of rat lung collectins that are essential for interactions with phospholipids, glycolipids, and alveolar type II cells
    • Sano H, Kuroki Y, Honma T, Ogasawara Y, Sohma H, Voelker DR, Akino T. Analysis of chimeric proteins identifies the regions in the carbohydrate recognition domains of rat lung collectins that are essential for interactions with phospholipids, glycolipids, and alveolar type II cells. J Biol Chem 1998;273:4783-4789.
    • (1998) J Biol Chem , vol.273 , pp. 4783-4789
    • Sano, H.1    Kuroki, Y.2    Honma, T.3    Ogasawara, Y.4    Sohma, H.5    Voelker, D.R.6    Akino, T.7
  • 22
    • 0001044156 scopus 로고    scopus 로고
    • The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
    • Ewart KV, Li Z, Yang DS, Fletcher GL, Hew CL. The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins. Biochemistry 1998;37:4080-4085.
    • (1998) Biochemistry , vol.37 , pp. 4080-4085
    • Ewart, K.V.1    Li, Z.2    Yang, D.S.3    Fletcher, G.L.4    Hew, C.L.5
  • 23
    • 0033064740 scopus 로고    scopus 로고
    • The amino acid sequence of ovocleidin 17, a major protein of the avian eggshell calcified layer
    • Mann K, Siedler F. The amino acid sequence of ovocleidin 17, a major protein of the avian eggshell calcified layer. Biochem Mol Biol Int 1999;47:997-1007.
    • (1999) Biochem Mol Biol Int , vol.47 , pp. 997-1007
    • Mann, K.1    Siedler, F.2
  • 24
    • 0034614599 scopus 로고    scopus 로고
    • Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata
    • Weiss IM, Kaufmann S, Mann K, Fritz M. Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata. Biochem Biophys Res Commun 2000;267:17-21.
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 17-21
    • Weiss, I.M.1    Kaufmann, S.2    Mann, K.3    Fritz, M.4
  • 25
    • 0031860633 scopus 로고    scopus 로고
    • Natural killer cell receptors
    • Yokoyama WM. Natural killer cell receptors. Curr Opin Immunol 1998;10:298-305.
    • (1998) Curr Opin Immunol , vol.10 , pp. 298-305
    • Yokoyama, W.M.1
  • 26
    • 0032006214 scopus 로고    scopus 로고
    • The lectin-like NK cell receptor Ly-49A recognizes a carbohydrate-independent epitope on its MHC class I ligand
    • Matsumoto N, Ribaudo RK, Abastado JP, Margulies DH, Yokoyama WM. The lectin-like NK cell receptor Ly-49A recognizes a carbohydrate-independent epitope on its MHC class I ligand. Immunity 1998;8:245-254.
    • (1998) Immunity , vol.8 , pp. 245-254
    • Matsumoto, N.1    Ribaudo, R.K.2    Abastado, J.P.3    Margulies, D.H.4    Yokoyama, W.M.5
  • 27
    • 0036234727 scopus 로고    scopus 로고
    • CD23 (the low-affinity IgE receptor) as a C-type lectin: A multidomain and multifunctional molecule
    • Kijimoto-Ochiai S. CD23 (the low-affinity IgE receptor) as a C-type lectin: a multidomain and multifunctional molecule. Cell Mol Life Sci 2002;59:648-664.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 648-664
    • Kijimoto-Ochiai, S.1
  • 29
    • 0034486070 scopus 로고    scopus 로고
    • The identification of conserved interactions within the SH3 domain by alignment of sequences and structures
    • Larson SM, Davidson AR. The identification of conserved interactions within the SH3 domain by alignment of sequences and structures. Protein Sci 2000;9:2170-2180.
    • (2000) Protein Sci , vol.9 , pp. 2170-2180
    • Larson, S.M.1    Davidson, A.R.2
  • 30
    • 0023176681 scopus 로고
    • Determinants of a protein fold: Unique features of the globin amino acid sequences
    • Bashford D, Chothia C, Lesk AM. Determinants of a protein fold: Unique features of the globin amino acid sequences. J Mol Biol 1987;196:199-216.
    • (1987) J Mol Biol , vol.196 , pp. 199-216
    • Bashford, D.1    Chothia, C.2    Lesk, A.M.3
  • 31
    • 0032080047 scopus 로고    scopus 로고
    • Structural determinants in the sequences of immunoglobulin variable domain
    • Chothia C, Gelfand I, Kister A. Structural determinants in the sequences of immunoglobulin variable domain. J Mol Biol 1998;278:457-479.
    • (1998) J Mol Biol , vol.278 , pp. 457-479
    • Chothia, C.1    Gelfand, I.2    Kister, A.3
  • 32
    • 0035667230 scopus 로고    scopus 로고
    • Structural similarity and functional diversity in proteins containing the legume lectin fold
    • Chandra NR, Prabu MM, Suguna K, Vijayan M. Structural similarity and functional diversity in proteins containing the legume lectin fold. Protein Eng 2001;14:857-866.
    • (2001) Protein Eng , vol.14 , pp. 857-866
    • Chandra, N.R.1    Prabu, M.M.2    Suguna, K.3    Vijayan, M.4
  • 33
    • 0035576329 scopus 로고    scopus 로고
    • Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes
    • Galperin MY, Jedrzejas MJ. Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes. Proteins 2001;45:318-324.
    • (2001) Proteins , vol.45 , pp. 318-324
    • Galperin, M.Y.1    Jedrzejas, M.J.2
  • 34
    • 0029962944 scopus 로고    scopus 로고
    • Conservation and variability in the structures of serine proteinases of the chymotrypsin family
    • Lesk AM, Fordham WD. Conservation and variability in the structures of serine proteinases of the chymotrypsin family. J Mol Biol 1996;258:501-537.
    • (1996) J Mol Biol , vol.258 , pp. 501-537
    • Lesk, A.M.1    Fordham, W.D.2
  • 35
    • 0033815279 scopus 로고    scopus 로고
    • Collectin structure: A review
    • Hakansson K, Reid KB. Collectin structure: A review. Protein Sci 2000;9:1607-1617.
    • (2000) Protein Sci , vol.9 , pp. 1607-1617
    • Hakansson, K.1    Reid, K.B.2
  • 36
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis WI, Taylor ME, Drickamer K. The C-type lectin superfamily in the immune system. Immunol Rev 1998;163:19-34.
    • (1998) Immunol Rev , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 37
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B. Twilight zone of protein sequence alignments. Protein Eng 1999;12:85-94.
    • (1999) Protein Eng , vol.12 , pp. 85-94
    • Rost, B.1
  • 38
    • 0035827172 scopus 로고    scopus 로고
    • Yet another numbering scheme for immunoglobulin variable domains: An automatic modeling and analysis tool
    • Honegger A, Pluckthun A. Yet another numbering scheme for immunoglobulin variable domains: An automatic modeling and analysis tool. J Mol Biol 2001;309:657-670.
    • (2001) J Mol Biol , vol.309 , pp. 657-670
    • Honegger, A.1    Pluckthun, A.2
  • 39
    • 0029982530 scopus 로고    scopus 로고
    • The structural alignment between two proteins: Is there a unique answer?
    • Godzik A. The structural alignment between two proteins: is there a unique answer? Protein Sci 1996;5:1325-1338.
    • (1996) Protein Sci , vol.5 , pp. 1325-1338
    • Godzik, A.1
  • 40
    • 0037103044 scopus 로고    scopus 로고
    • Comparison of sequence and structure alignments for protein domains
    • Marchler-Bauer A, Panchenko AR, Ariel N, Bryant SH. Comparison of sequence and structure alignments for protein domains. Proteins 2002;48:439-446.
    • (2002) Proteins , vol.48 , pp. 439-446
    • Marchler-Bauer, A.1    Panchenko, A.R.2    Ariel, N.3    Bryant, S.H.4
  • 41
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov IN, Bourne PE. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng 1998;11:739-747.
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 42
    • 0030628304 scopus 로고    scopus 로고
    • Hierarchical protein structure superposition using both secondary structure and atomic representations
    • Singh AP, Brutlag DL. Hierarchical protein structure superposition using both secondary structure and atomic representations. Proc Int Conf Intell Syst Mol Biol 1997;5:284-293.
    • (1997) Proc Int Conf Intell Syst Mol Biol , vol.5 , pp. 284-293
    • Singh, A.P.1    Brutlag, D.L.2
  • 43
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 44
    • 0027504807 scopus 로고
    • Regularities in interaction patterns of globular proteins
    • Godzik A, Skolnick J, Kolinski A. Regularities in interaction patterns of globular proteins. Protein Eng 1993;6:801-810.
    • (1993) Protein Eng , vol.6 , pp. 801-810
    • Godzik, A.1    Skolnick, J.2    Kolinski, A.3
  • 45
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 46
    • 0026342532 scopus 로고
    • Information-theoretical entropy as a measure of sequence variability
    • Shenkin PS, Erman B, Mastrandrea LD. Information-theoretical entropy as a measure of sequence variability. Proteins 1991;11:297-313.
    • (1991) Proteins , vol.11 , pp. 297-313
    • Shenkin, P.S.1    Erman, B.2    Mastrandrea, L.D.3
  • 49
    • 0035072551 scopus 로고    scopus 로고
    • Clustering of highly homologous sequences to reduce the size of large protein databases
    • Li W, Jaroszewski L, Godzik A. Clustering of highly homologous sequences to reduce the size of large protein databases. Bioinformatics 2001;17:282-283.
    • (2001) Bioinformatics , vol.17 , pp. 282-283
    • Li, W.1    Jaroszewski, L.2    Godzik, A.3
  • 50
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 51
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR. Profile hidden Markov models. Bioinformatics 1998;14:755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 52
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C. Mapping the protein universe. Science 1996;273:595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 53
    • 0034697981 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor
    • Meier M, Bider MD, Malashkevich VN, Spiess M, Burkhard P. Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. J Mol Biol 2000;300:857-865.
    • (2000) J Mol Biol , vol.300 , pp. 857-865
    • Meier, M.1    Bider, M.D.2    Malashkevich, V.N.3    Spiess, M.4    Burkhard, P.5
  • 56
    • 0033540084 scopus 로고    scopus 로고
    • Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand
    • Tormo J, Natarajan K, Margulies DH, Mariuzza RA. Crystal structure of a lectin-like natural killer cell receptor bound to its MHC class I ligand. Nature 1999;402:623-631.
    • (1999) Nature , vol.402 , pp. 623-631
    • Tormo, J.1    Natarajan, K.2    Margulies, D.H.3    Mariuzza, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.