1JSS

Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4).

Summary for 1JSS

• Entry DOI: 10.2210/pdb1jss/pdb
• Descriptor: cholesterol-regulated START protein 4 (2 entities in total)
• Functional Keywords: start domain, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, lipid binding protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 51159.89

Authors

Romanowski, M.J.,Soccio, R.E.,Breslow, J.L.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2001-08-17, release date: 2002-04-10, Last modification date: 2024-02-07)

Primary citation

Romanowski, M.J.,Soccio, R.E.,Breslow, J.L.,Burley, S.K.
Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain.
Proc.Natl.Acad.Sci.USA, 99:6949-6954, 2002

PubMed 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.

PubMed: 12011453
DOI: 10.1073/pnas.052140699

Experimental method

X-RAY DIFFRACTION (2.2 Å)