| Structure of human erythrocyte spectrin. II. The sequence of the alpha-I domain. | |
| | |
MedLine Citation:
|
PMID: 6654896 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
The complete sequence of 595 amino acids of the alpha-I domain of human erythrocyte spectrin has been determined. Peptides derived from three different protease cleavages were purified using high performance liquid chromatography and subjected to automated amino acid sequence analysis. These data along with sequences of the cyanogen bromide and large tryptic peptides (Speicher, D.W., Davis, G., Yurchenco, P.D., and Marchesi, V.T. (1983) J. Biol. Chem. 258, 14931-14937) represent most or all of the sequence of spectrin alpha-I. The single remaining ambiguity is the precise termination of the COOH terminus of the alpha-I domain. The sequence data suggest that the 595 residues presented here represent the complete sequence of the alpha-I domain, but the apparent size of the COOH-terminal CNBr fragment suggests the existence of an additional 38 residues at the end of the domain. The sequence of the alpha-I domain contains a single type of internal homology composed of multiple 106-amino acid repeats consistent with the occurrence of multiple gene duplications during the course of spectrin evolution. The only portion of the alpha-I sequence which does not appear to contain this sequence repeat is the segment containing the NH2-terminal 17 residues. This unique segment may be part of the oligomer binding site. No disulfide bonds appear to be involved in the structure of alpha-I and cysteine is not highly conserved. Calculations of secondary structure suggest the presence of short helices which fold into triple helical segments approximately 50 A in length. There is little beta sheet structure. A model of spectrin structure incorporating the repeat unit and proposed secondary structure is presented. A computer search of alpha-I sequence with the National Biomedical Research Foundation database of 2145 protein sequences did not detect any significant relationships. Spectrin is apparently the first member of a new class of proteins to be structurally characterized. |
| | |
Authors:
|
D W Speicher; G Davis; V T Marchesi |
Related Documents
:
|
8925896 - The spectrin repeat folds into a three-helix bundle in solution. 23176826 - Probing the energetic and kinetic impact of topologically conserved interactions in the... 11135986 - Monitor-outside-a-monitor effect and self-similar fractal structure in the eigenmodes o... 12176386 - Pathways and intermediates in forced unfolding of spectrin repeats. 21030956 - Synthesis of peptide macrocycles using unprotected amino aldehydes. 9657386 - Substrate-dependent activation requirements and kinetic properties of protein kinase c. |
Publication Detail:
|
Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
|
Title: The Journal of biological chemistry Volume: 258 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 1983 Dec |
Date Detail:
|
Created Date: 1984-02-14 Completed Date: 1984-02-14 Revised Date: 2007-11-14 |
Medline Journal Info:
|
Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
|
Languages: eng Pagination: 14938-47 Citation Subset: IM |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Erythrocytes / analysis Humans Protein Conformation Spectrin / analysis* |
| Grant Support | |
ID/Acronym/Agency:
|
AM27932/AM/NIADDK NIH HHS; GM21714/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
|
12634-43-4/Spectrin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Structure of human erythrocyte spectrin. I. Isolation of the alpha-I domain and its cyanogen bromide...
Next Document: Ascorbic acid is an endogenous cytosolic inhibitor of ATP-supported rat liver mitochondrial calcium ...