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1kmx
From Proteopedia
Heparin-binding Domain from Vascular Endothelial Growth Factor
Previous NMR structural studies of the heparin-binding domain of vascular endothelial growth factor (VEGF165) revealed a novel fold comprising two subdomains, each containing two disulfide bridges and a short two-stranded antiparallel beta-sheet. The mutual orientation of the two subdomains was poorly defined by the NMR data. Heteronuclear relaxation data suggested that this disorder resulted from a relative lack of experimental restraints due to the limited size of the interface, rather than inherent high-frequency flexibility. Refinement of the structure using 1H(N-15N residual dipolar coupling restraints results in significantly improved definition of the relative subdomain orientations.
Refinement of the solution structure of the heparin-binding domain of vascular endothelial growth factor using residual dipolar couplings., Stauffer ME, Skelton NJ, Fairbrothe WJ, J Biomol NMR. 2002 May;23(1):57-61. PMID:12061718
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1KMX is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
See VEGF for additional structural information.
Reference
- Stauffer ME, Skelton NJ, Fairbrothe WJ. Refinement of the solution structure of the heparin-binding domain of vascular endothelial growth factor using residual dipolar couplings. J Biomol NMR. 2002 May;23(1):57-61. PMID:12061718
Page seeded by OCA on Tue Feb 17 08:04:59 2009
