PUBLICATION
Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain
- Authors
- Romanowski, M.J., Soccio, R.E., Breslow, J.L., and Burley, S.K.
- ID
- ZDB-PUB-031105-4
- Date
- 2002
- Source
- Proceedings of the National Academy of Sciences of the United States of America 99(10): 6949-6954 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Models, Molecular
- Crystallography, X-Ray
- Phosphoproteins
- Sequence Analysis
- Animals
- Humans
- Mice
- Protein Structure, Tertiary
- Carrier Proteins/chemistry*
- Carrier Proteins/classification
- Carrier Proteins/genetics
- Cholesterol/metabolism*
- Amino Acid Sequence
- Membrane Transport Proteins*
- Molecular Sequence Data
- Phylogeny
- Sequence Homology, Amino Acid
- Computer Simulation
- PubMed
- 12011453 Full text @ Proc. Natl. Acad. Sci. USA
Citation
Romanowski, M.J., Soccio, R.E., Breslow, J.L., and Burley, S.K. (2002) Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain. Proceedings of the National Academy of Sciences of the United States of America. 99(10):6949-6954.
Abstract
The x-ray structure of the mouse cholesterol-regulated START protein 4 (StarD4) has been determined at 2.2-A resolution, revealing a compact alpha/beta structure related to the START domain present in the cytoplasmic C-terminal portion of human MLN64. The volume of the putative lipid-binding tunnel was estimated at 847 A(3), which is consistent with the binding of one cholesterol-size lipid molecule. Comparison of the tunnel-lining residues in StarD4 and MLN64-START permitted identification of possible lipid specificity determinants in both molecular tunnels. Homology modeling of related proteins, and comparison of the StarD4 and MLN64-START structures, showed that StarD4 is a member of a large START domain superfamily characterized by the helix-grip fold. Additional mechanistic and evolutionary studies should be facilitated by the availability of a second START domain structure from a distant relative of MLN64.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping