1ha1
From Proteopedia
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'''HNRNP A1 (RBD1,2) FROM HOMO SAPIENS''' | '''HNRNP A1 (RBD1,2) FROM HOMO SAPIENS''' | ||
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[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
[[Category: Williams, K R.]] | [[Category: Williams, K R.]] | ||
- | [[Category: | + | [[Category: Hnrnp]] |
- | [[Category: | + | [[Category: Nuclear protein]] |
- | [[Category: | + | [[Category: Rbd]] |
- | [[Category: | + | [[Category: Ribonucleoprotein]] |
- | [[Category: | + | [[Category: Rna binding]] |
- | [[Category: | + | [[Category: Rnp]] |
- | [[Category: | + | [[Category: Rrm]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:37:26 2008'' | |
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Revision as of 15:37, 2 May 2008
HNRNP A1 (RBD1,2) FROM HOMO SAPIENS
Overview
Heterogeneous ribonucleoprotein A1 (hnRNP A1) is an abundant eukaryotic nuclear RNA binding protein. A1 is involved in the packaging of pre-mRNA into hnRNP particles, transport of poly A+ mRNA from the nucleus to the cytoplasm and may modulate splice site selection. The crystal structure of A1(RBD1,2) reveals two independently-folded RNA binding domains (RBDs) connected by a flexible linker. Both RBDs are structurally homologous to the U1A(RBD1), and have their RNA binding platforms oriented in an anti-parallel fashion. The anti-parallel arrangement of the A1 RNA binding platforms suggests mechanisms for RNA condensation and ways of bringing together distant RNA sequences for RNA metabolism such as splicing or transport.
About this Structure
1HA1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 A resolution., Shamoo Y, Krueger U, Rice LM, Williams KR, Steitz TA, Nat Struct Biol. 1997 Mar;4(3):215-22. PMID:9164463 Page seeded by OCA on Fri May 2 18:37:26 2008
Categories: Homo sapiens | Single protein | Krueger, U. | Rice, L. | Shamoo, Y. | Steitz, T A. | Williams, K R. | Hnrnp | Nuclear protein | Rbd | Ribonucleoprotein | Rna binding | Rnp | Rrm