Trimerization of the Amino Propeptide of Type IIA Procollagen Using a 14-Amino Acid Sequence Derived from the Coiled-Coil Neck Domain of Surfactant Protein D

Human pulmonary surfactant protein D (SP-D) was identified in lung lavage by its similarity to rat SP-D in both its molecular mass and its Ca(2+)-dependent-binding affinity for maltose [Persson, Chang & Crouch (1990) J. Biol. Chem. 265, 5755-5760]. For structural studies, human SP-D was isolated from amniotic fluid by affinity chromatography on maltose-Sepharose followed by f.p.l.c. on Superose 6, which showed it to have a molecular mass of approx. 620 kDa in non-dissociating conditions. On SDS/PAGE the human SP-D behaved as a single band of 150 kDa or 43 kDa in non-reducing or reducing conditions respectively. The presence of a high concentration of glycine (22%), hydroxyproline and hydroxylysine in the amino acid composition of human SP-D indicated that it contained collagen-like structure. Collagenase digestion yielded a 20 kDa collagenase-resistant globular fragment which retained affinity for maltose. Use of maltosyl-BSA as a neoglycoprotein ligand in a solid-phase binding assay showed that human SP-D has a similar carbohydrate-binding specificity to rat SP-D, but a clearly distinct specificity from that of other lectins, such as conglutinin, for a range of simple saccharides. Amino acid sequence analysis established the presence of collagen-like Gly-Xaa-Yaa triplets in human SP-D and also provided sequence data from the globular region of the molecule which was used in the synthesis of oligonucleotide probes. Screening of a human lung cDNA library with the oligonucleotide probes, and also with rabbit anti-(human SP-D), allowed the isolation of two cDNA clones which overlap to give the full coding sequence of human SP-D. The derived amino acid sequence indicates that the mature human SP-D polypeptide chain is 355 residues long, having a short non-collagen-like N-terminal section of 25 residues, followed by a collagen-like region of 177 residues and a C-terminal C-type lectin domain of 153 residues. Comparison of the human SP-D and bovine serum conglutinin amino acid sequences indicated that they showed 66% identity despite their marked differences in carbohydrate specificity.

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The Amino-terminal Heptad Repeats of the Coiled-coil Neck Domain of Pulmonary Surfactant Protein D Are Necessary for the Assembly of Trimeric Subunits and Dodecamers

Journal of Biological Chemistry ◽

10.1074/jbc.m100597200 ◽

2001 ◽

Vol 276 (23) ◽

pp. 19862-19870 ◽

Cited By ~ 33

Author(s):

Pengnian Zhang ◽

Audrey McAlinden ◽

Shi Li ◽

Troy Schumacher ◽

Hongling Wang ◽

...

Keyword(s):

Pulmonary Surfactant ◽

Coiled Coil ◽

Surfactant Protein ◽

Surfactant Protein D ◽

Amino Terminal ◽

Neck Domain ◽

Heptad Repeats ◽

Pulmonary Surfactant Protein

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The Coiled-Coil Neck Domain of Human Pulmonary Surfactant Protein D Drives Trimerization and Stabilization of Thioredoxin, a Heterologous Non-Collagenous Protein

Protein and Peptide Letters ◽

10.2174/092986609787601769 ◽

2009 ◽

Vol 16 (3) ◽

pp. 306-311

Author(s):

Ping Li ◽

Jian Zhou ◽

Yin Zhou ◽

Chao Qian ◽

Ou Li ◽

...

Keyword(s):

Pulmonary Surfactant ◽

Coiled Coil ◽

Surfactant Protein ◽

Surfactant Protein D ◽

Neck Domain ◽

Pulmonary Surfactant Protein

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Conserved DNA binding and self-association domains of the Drosophila zeste protein

Molecular and Cellular Biology ◽

10.1128/mcb.12.2.598-608.1992 ◽

1992 ◽

Vol 12 (2) ◽

pp. 598-608

Author(s):

J D Chen ◽

C S Chan ◽

V Pirrotta

Keyword(s):

Amino Acid ◽

Dna Binding ◽

Amino Acid Sequence ◽

Coiled Coil ◽

Helical Structure ◽

Binding Activity ◽

Binding Domain ◽

Drosophila Virilis ◽

Predicted Amino Acid Sequence ◽

Dna Binding Domain

The zeste gene product is involved in two types of genetic effects dependent on chromosome pairing: transvection and the zeste-white interaction. Comparison of the predicted amino acid sequence with that of the Drosophila virilis gene shows that several blocks of amino acid sequence have been very highly conserved. One of these regions corresponds to the DNA binding domain. Site-directed mutations in this region indicate that a sequence resembling that of the homeodomain DNA recognition helix is essential for DNA binding activity. The integrity of an amphipathic helical region is also essential for binding activity and is likely to be responsible for dimerization of the DNA binding domain. Another very strongly conserved domain of zeste is the C-terminal region, predicted to form a long helical structure with two sets of heptad repeats that constitute two long hydrophobic ridges at opposite ends and on opposite faces of the helix. We show that this domain is responsible for the extensive aggregation properties of zeste that are required for its role in transvection phenomena. A model is proposed according to which the hydrophobic ridges induce the formation of open-ended coiled-coil structures holding together many hundreds of zeste molecules and possibly anchoring these complexes to other nuclear structures.

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Conserved DNA binding and self-association domains of the Drosophila zeste protein.

Molecular and Cellular Biology ◽

10.1128/mcb.12.2.598 ◽

1992 ◽

Vol 12 (2) ◽

pp. 598-608 ◽

Cited By ~ 15

Author(s):

J D Chen ◽

C S Chan ◽

V Pirrotta

Keyword(s):

Amino Acid ◽

Dna Binding ◽

Amino Acid Sequence ◽

Coiled Coil ◽

Helical Structure ◽

Binding Activity ◽

Binding Domain ◽

Drosophila Virilis ◽

Predicted Amino Acid Sequence ◽

Dna Binding Domain

The zeste gene product is involved in two types of genetic effects dependent on chromosome pairing: transvection and the zeste-white interaction. Comparison of the predicted amino acid sequence with that of the Drosophila virilis gene shows that several blocks of amino acid sequence have been very highly conserved. One of these regions corresponds to the DNA binding domain. Site-directed mutations in this region indicate that a sequence resembling that of the homeodomain DNA recognition helix is essential for DNA binding activity. The integrity of an amphipathic helical region is also essential for binding activity and is likely to be responsible for dimerization of the DNA binding domain. Another very strongly conserved domain of zeste is the C-terminal region, predicted to form a long helical structure with two sets of heptad repeats that constitute two long hydrophobic ridges at opposite ends and on opposite faces of the helix. We show that this domain is responsible for the extensive aggregation properties of zeste that are required for its role in transvection phenomena. A model is proposed according to which the hydrophobic ridges induce the formation of open-ended coiled-coil structures holding together many hundreds of zeste molecules and possibly anchoring these complexes to other nuclear structures.

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The amino acid sequence of component 7c, a type II intermediate-filament protein from wool

Biochemical Journal ◽

10.1042/bj2611015 ◽

1989 ◽

Vol 261 (3) ◽

pp. 1015-1022 ◽

Cited By ~ 26

Author(s):

L G Sparrow ◽

C P Robinson ◽

D T W McMahon ◽

M R Rubira

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Intermediate Filament ◽

Coiled Coil ◽

British Library ◽

Intermediate Filament Protein ◽

Type I ◽

Type Ii ◽

Blocking Group ◽

Intermediate Filament Proteins

Component 7c is one of the four homologous type II intermediate-filament proteins that, by association with the complementary type I proteins, form the microfibrils or intermediate filaments in wool. Component 7c was isolated as the S-carboxymethyl derivative from Merino wool and its amino acid sequence was determined by manual and automatic sequencing of peptides produced by chemical and enzymic cleavage reactions. It is an N-terminally blocked molecule of 491 residues and Mr (not including the blocking group) of 55,600; the nature of the blocking group has not been determined. The predicted secondary structure shows that component 7c conforms to the now accepted pattern for intermediate-filament proteins in having a central rod-like region of approximately 310 residues of coiled-coil alpha-helix flanked by non-helical N-and C-terminal regions. The central region is divided by three non-coiled-coil linking segments into four helical segments 1A, 1B, 2A and 2B. The N-and C-terminal non-helical segments are 109 and 71 residues respectively and are rich in cysteine. Details of procedures use in determining the sequence of component 7c have been deposited as a Supplementary Publication SUP 50152 (65 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257,5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 7c, peptides CN1, CN2 and CN3, and various other peptides, (2) details of the procedures used for the fractionation and purification of peptides from (1), including Figures showing the elution profiles from the chromatographic steps used, (3) details of methods used to determine the C-terminal sequence of peptide CN3, and (4) detailed evidence to justify a number of corrections to the previously published sequence.

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