1shf
From Proteopedia
(Difference between revisions)
m (Protected "1shf" [edit=sysop:move=sysop]) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | [[1shf]] is a 2 chain structure | + | [[1shf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHF OCA]. |
==See Also== | ==See Also== | ||
| Line 14: | Line 14: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:007687536 | + | <ref group="xtra">PMID:007687536</ref><ref group="xtra">PMID:016142914</ref><ref group="xtra">PMID:016477599</ref><ref group="xtra">PMID:019170498</ref><references group="xtra"/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 19:13, 20 October 2012
Contents |
CRYSTAL STRUCTURE OF THE SH3 DOMAIN IN HUMAN FYN; COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF SH3 DOMAINS IN TYROSINE KINASES AND SPECTRIN
Template:ABSTRACT PUBMED 7687536
About this Structure
1shf is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Noble ME, Musacchio A, Saraste M, Courtneidge SA, Wierenga RK. Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin. EMBO J. 1993 Jul;12(7):2617-24. PMID:7687536
- de los Rios MA, Daneshi M, Plaxco KW. Experimental investigation of the frequency and substitution dependence of negative phi-values in two-state proteins. Biochemistry. 2005 Sep 13;44(36):12160-7. PMID:16142914 doi:10.1021/bi0505621
- Huang JT, Tian J. Amino acid sequence predicts folding rate for middle-size two-state proteins. Proteins. 2006 May 15;63(3):551-4. PMID:16477599 doi:10.1002/prot.20911
- Zhang F, Zarrine-Afsar A, Al-Abdul-Wahid MS, Prosser RS, Davidson AR, Woolley GA. Structure-based approach to the photocontrol of protein folding. J Am Chem Soc. 2009 Feb 18;131(6):2283-9. PMID:19170498 doi:10.1021/ja807938v
