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Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.

The three-dimensional structure of human basic fibroblast growth factor has been refined to a crystallographic residual of 16.1% at 1.6 A resolution. The structure has a Kunitz-type fold and is composed of 12 antiparallel beta-strands, 6 of which form a beta-barrel. One bound sulfate ion has been id...

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Autori principali: Eriksson, A. E., Cousens, L. S., Matthews, B. W.
Natura: Artigo
Lingua:Inglês
Pubblicazione: Cold Spring Harbor Laboratory Press 1993
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142437/
https://ncbi.nlm.nih.gov/pubmed/7691311
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