Determinants of quaternary association in legume lectins

被引:60
作者
Brinda, KV [1 ]
Mitra, N [1 ]
Surolia, A [1 ]
Vishveshwara, S [1 ]
机构
[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India
关键词
computational protein structure analysis; quaternary association; oligomerization; legume lectins; graph-spectral method; interface amino acid clusters; conserved amino acid clusters;
D O I
10.1110/ps.04651004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
It is well known that the sequence of amino acids in proteins code for its tertiary structure. It is also known that there exists a relationship between sequence and the quaternary structure of proteins. The question addressed here is whether the nature of quaternary association can be predicted from the sequence, similar to the three-dimensional structure prediction from the sequence. The class of proteins called legume lectins is an interesting model system to investigate this problem, because they have very high sequence and tertiary structure homology, with diverse forms of quaternary association. Hence, we have used legume lectins as a probe in this paper to (1) gain novel insights about the relationship between sequence and quaternary structure; (2) identify the sequence motifs that are characteristic of a given type of quaternary association; and (3) predict the quaternary association from the sequence motif.
引用
收藏
页码:1735 / 1749
页数:15
相关论文
共 26 条
[1]
[Anonymous], 1986, LECTINS PROPERTIES F
[2]
CRYSTAL-STRUCTURE OF PEANUT LECTIN, A PROTEIN WITH AN UNUSUAL QUATERNARY STRUCTURE [J].
BANERJEE, R ;
MANDE, SC ;
GANESH, V ;
DAS, K ;
DHANARAJ, V ;
MAHANTA, SK ;
SUGUNA, K ;
SUROLIA, A ;
VIJAYAN, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (01) :227-231
[3]
The Protein Data Bank [J].
Berman, HM ;
Westbrook, J ;
Feng, Z ;
Gilliland, G ;
Bhat, TN ;
Weissig, H ;
Shindyalov, IN ;
Bourne, PE .
NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242
[4]
The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003 [J].
Boeckmann, B ;
Bairoch, A ;
Apweiler, R ;
Blatter, MC ;
Estreicher, A ;
Gasteiger, E ;
Martin, MJ ;
Michoud, K ;
O'Donovan, C ;
Phan, I ;
Pilbout, S ;
Schneider, M .
NUCLEIC ACIDS RESEARCH, 2003, 31 (01) :365-370
[5]
Analysis of homodimeric protein interfaces by graph-spectral methods [J].
Brinda, KV ;
Kannan, N ;
Vishveshwara, S .
PROTEIN ENGINEERING, 2002, 15 (04) :265-277
[6]
Weak protein-protein interactions in lectins:: the crystal structure of a vegetative lectin from the legume Dolichos biflorus [J].
Buts, L ;
Dao-Thi, MH ;
Loris, R ;
Wyns, L ;
Etzler, M ;
Hamelryck, T .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 309 (01) :193-201
[7]
Amino acid sequence, glycan structure, and proteolytic processing of the lectin of Vatairea macrocarpa seeds [J].
Calvete, JJ ;
Santos, CF ;
Mann, K ;
Grangeiro, TB ;
Nimtz, M ;
Urbanke, C ;
Cavada, BS .
FEBS LETTERS, 1998, 425 (02) :286-292
[8]
Electron microscopy and X-ray diffraction studies of Lotus tetragonolobus A isolectin cross-linked with a divalent Lewisx oligosaccharide, an oncofetal antigen [J].
Cheng, W ;
Bullitt, E ;
Bhattacharyya, L ;
Brewer, CF ;
Makowski, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (52) :35016-35022
[9]
Crystal structure of arcelin-5, a lectin-like defense protein from Phaseolus vulgaris [J].
Hamelryck, TW ;
Poortmans, F ;
Goossens, A ;
Angenon, G ;
VanMontagu, M ;
Wyns, L ;
Loris, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (51) :32796-32802
[10]
The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: Crystal structure of cross-linked FRIL [J].
Hamelryck, TW ;
Moore, JG ;
Chrispeels, MJ ;
Loris, R ;
Wyns, L .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 299 (04) :875-883